Progress 12/15/13 to 12/14/18

Outputs
Target Audience:- The research community studying the interaction of Pseudomonas syringae and other bacteria with plants. - Scientists that are breeding plants for increased resistance to pathogens. Changes/Problems: Nothing Reported What opportunities for training and professional development has the project provided?Funding from this grant has so far allowed for training of two graduate students, Incheol Yeo and Dongyin Su. These students are trained in molecular biology and biochemistry techniques to study plant interactions with pathogens. They were also trained in the writing and the publication process for having a scientific study published in an international scientific journal. Additional training includes reviewing manuscripts from scientific journals, creating poster and oral presentations for scientific meetings, developing networking opportunities, and communicating scientific findings to the public. How have the results been disseminated to communities of interest? Nothing Reported What do you plan to do during the next reporting period to accomplish the goals? Nothing Reported

Impacts
What was accomplished under these goals? Studies to identify the nuclear phosphorylation substrates of Adi3 using phosphoproteomics has been very challenging. Thus, over the past year we took a new approach of using peptide microarray chips. These chips contain 1,536 unique synthetic kinase peptide substrates. The peptides on the chips are phosphorylated by Adi3 using [32P]-ATP and peptides phosphorylated by Adi3 are identified by incorporation of 32P. During this process it took several months to optimize the phosphorylation of the peptide chip as there were many factors such as [32P]-ATP concentration, Adi3 concentration, and incubation time that affected the efficiency of phosphorylation. The results showed that Adi3 efficiently phosphorylated many of the peptides on the chip. Using the sequence of the 63 strongest Adi3 phosphorylated peptides to identify proteins with similar sequences to these peptides. Each peptide sequence was BLASTed against the tomato gene and protein databases and returned 1,068 proteins that contained at least 5 amino acids, including the phosphorylatable Ser, identical to any given peptide phosphorylated by Adi3. The highest match of a peptide sequence to a tomato protein was 10 amino acids, which was found for 5 different peptides. Most peptides matched 6 to 8 amino acids in the identified tomato proteins. This list of proteins was further narrowed down to 413 possible candidate proteins based on predicted nuclear localization or relevance to pathogen resistance. This list has been further narrowed to a top 10 list of proteins to be analyzed for Adi3 phosphorylation based on nuclear function and relevance to pathogen resistance. The list includes proteins with functions in chromatin remodeling, transcription regulation, and RNA polymerase. We are currently analyzing Adi3 phosphorylation of these potential substrates. Additionally, this grant has allowed us to pursue a new avenue for deciphering the resistance mechanisms employed by tomato for defense against P. syringae. We have found that the enzyme threonine deaminase 2 (TD2) is posttranslationally modified in response to P. syringae flg22. The deamination of threonine by TD2 to form alpha-ketobutyrate has been shown to be the rate limiting step in the production of isoleucine (Ile). This Ile can then be used for conjugation to the defense hormone jasmonic acid to generate the active form of jasmonic acid, JA-Ile, for defense against insect herbivores and necrotrophic pathogens. Since JA-Ile can interfere with the salicylic acid (SA) based defenses needed for resistance to P. syringae, plants inhibit JA-Ile-induced gene expression during P. syringae resistance. We have found that in response to flg22 TD2 is posttranslationally PARylated, the addition of poly(ADP-ribose) to the protein, this occurs within the first 5 minutes after flg22 detection and is followed by removal of the PARylation by 24 hours after flg22 detection. Our working hypothesis is that TD2 PARylation inhibits TD2 enzyme activity preventing production of the Ile needed for JA-Ile biosynthesis. Thus, the amount of JA-Ile is reduced to prevent interference with the needed SA defense responses. A role for TD2 in the tomato defense response against P. syringae has not yet been shown and our discovery of a potential involvement of TD in the basal defense response to P. syringae flagellin opens an exciting new area of research.

Publications

Progress 12/15/16 to 12/14/17

Outputs
Target Audience:- The research community studying the interaction of Pseudomonas syringae and other bacteria with plants.? - Scientists that are breeding plants for increased resistance to pathogens. Changes/Problems: Nothing Reported What opportunities for training and professional development has the project provided?Under these studies training training of two graduate students, Incheol Yeo and Dongyin Su. These students are trained in molecular biology and biochemistry techniques to study plant interactions with pathogens. They were also trained in the writing and the publication process for having a scientific study published in an international scientific journal. Additional training includes reviewing manuscripts from scientific journals, creating poster and oral presentations for scientific meetings, developing networking opportunities, and communicating scientific findings to the public How have the results been disseminated to communities of interest? Nothing Reported What do you plan to do during the next reporting period to accomplish the goals? Nothing Reported

Impacts
What was accomplished under these goals? Studies to identify the nuclear phosphorylation substrates of Adi3 using phosphoproteomics has been very challenging. Thus, over the past year we took a new approach of using peptide microarray chips. These chips contain 1,536 unique synthetic kinase peptide substrates. The peptides on the chips are phosphorylated by Adi3 using [32P]-ATP and peptides phosphorylated by Adi3 are identified by incorporation of 32P. During this process it took several months to optimize the phosphorylation of the peptide chip as there were many factors such as [32P]-ATP concentration, Adi3 concentration, and incubation time that affected the efficiency of phosphorylation. The results showed that Adi3 efficiently phosphorylated many of the peptides on the chip. Using the sequence of the 63 strongest Adi3 phosphorylated peptides to identify proteins with similar sequences to these peptides. Each peptide sequence was BLASTed against the tomato gene and protein databases and returned 1,068 proteins that contained at least 5 amino acids, including the phosphorylatable Ser, identical to any given peptide phosphorylated by Adi3. The highest match of a peptide sequence to a tomato protein was 10 amino acids, which was found for 5 different peptides. Most peptides matched 6 to 8 amino acids in the identified tomato proteins. This list of proteins was further narrowed down to 413 possible candidate proteins based on predicted nuclear localization or relevance to pathogen resistance. This list has been further narrowed to a top 10 list of proteins to be analyzed for Adi3 phosphorylation based on nuclear function and relevance to pathogen resistance. The list includes proteins with functions in chromatin remodeling, transcription regulation, and RNA polymerase. We are currently analyzing Adi3 phosphorylation of these potential substrates. Additionally, this grant has allowed us to pursue a new avenue for deciphering the resistance mechanisms employed by tomato for defense against P. syringae. We have found that the enzyme threonine deaminase 2 (TD2) is posttranslationally modified in response to P. syringae flg22. The deamination of threonine by TD2 to form alpha-ketobutyrate has been shown to be the rate limiting step in the production of isoleucine (Ile). This Ile can then be used for conjugation to the defense hormone jasmonic acid to generate the active form of jasmonic acid, JA-Ile, for defense against insect herbivores and necrotrophic pathogens. Since JA-Ile can interfere with the salicylic acid (SA) based defenses needed for resistance to P. syringae, plants inhibit JA-Ile-induced gene expression during P. syringae resistance. We have found that in response to flg22 TD2 is posttranslationally PARylated, the addition of poly(ADP-ribose) to the protein, this occurs within the first 5 minutes after flg22 detection and is followed by removal of the PARylation by 24 hours after flg22 detection. Our working hypothesis is that TD2 PARylation inhibits TD2 enzyme activity preventing production of the Ile needed for JA-Ile biosynthesis. Thus, the amount of JA-Ile is reduced to prevent interference with the needed SA defense responses. A role for TD2 in the tomato defense response against P. syringae has not yet been shown and our discovery of a potential involvement of TD in the basal defense response to P. syringae flagellin opens an exciting new area of research.

Publications

Progress 12/15/15 to 12/14/16

Outputs
Target Audience:- The research community studying the interaction of Pseudomonas syringae and other bacteria with plants. - Scientists that are breeding plants for increased resistance to pathogens. Changes/Problems: Nothing Reported What opportunities for training and professional development has the project provided?Funding from this grant has so far allowed for training of two graduate students, Incheol Yeo and Dongyin Su. These students are trained in molecular biology and biochemistry techniques to study plant interactions with pathogens. They were also trained in the writing and the publication process for having a scientific study published in an international scientific journal. Additional training includes reviewing manuscripts from scientific journals, creating poster and oral presentations for scientific meetings, developing networking opportunities, and communicating scientific findings to the public. How have the results been disseminated to communities of interest? Over the past year our studies on cell death control and its role in resistance to P. syringae have been disseminated to the general scientific public through the presentation of three posters at Plant Biology 2016, the annual meeting of the American Society of Plant Biologists, Austin, TX. July, 2016. We have also published one paper in the New Phytologist from a collaboration with Dr. Fangming Xiao at the University of Idaho. What do you plan to do during the next reporting period to accomplish the goals? In the next reporting period we will confirm Adi3 phosphorylation of the identified nuclear phosphorylation substrates. This will be accomplished by using mass spectrometry followed by mutation of the identified phosphorylation sites to non-phosphorylation Alanine to show loss of phosphorylation by Adi3. Once confirmed, the role of the phosphorylation on each candidate will be studied in relation to the predicted function of the phosphorylated protein as well as in the context of resistance to P. syringae. Several of the potential Adi3 phosphorylation substrates encode transcription factors or proteins involved in controlling the transcription process raising the possibility of alterations in gene transcription to control PCD in tomato during the resistance response to P. syringae. For the TD2 studies we will assess the role of phosphorylation/dephosphorylation on TD2 enzyme activity, identify the TD2 kinase and analyze its role in pathogen resistance, and use gene silencing techniques to assess the role of TD2 in basal resistance.

Impacts
What was accomplished under these goals? The major accomplishments involved the identification of potential nuclear protein phosphorylation substrates for Adi3. We faced many challenges using a phosphoproteomics and were not successful. Thus, we used peptide microarrays that have over 1,500 phosphorylatable synthetic peptides on a glass slide. The peptides are phosphorylated with Adi3 using [32P]-ATP and the sequence of the phosphorylated peptides are used to search the tomato proteome by BLAST to identify proteins containing amino acid sequences based on the phosphorylated peptides. The Ser peptide microarray chips contain 1,536 individual peptides. Each peptide contains 13 random; 6 amino acids on either side of a phosphorylatable Ser residue. The peptides are printed on the slide in 3 identical subarrays. Each subarray contains 1,536 peptides. Each subarray contains 16 sections and each section contains 96 peptides printed in triplicate. Thus, 16 sections times 96 peptides give 1,536 peptides in each subarray. In this manner, each peptide is printed on the slide 9 times (3 peptides in each subarray) to allow for reproducible results within a single chip. We used the Ser peptide chip for phosphorylation by a constitutively active form of Adi3. There were many parameters to optimize for the phosphorylation of the Ser peptide chip such as the amount of [32P]-ATP to use, the length of incubation for the kinase reactions, the amount of Adi3 kinase to use, and the temperature at which to incubate the reaction. Finding the optimal conditions took 4 attempts at phosphorylating the Ser peptide chip. The conditions used were much different from our typical in vitro Adi3 kinase assay and required 10 times more Adi3 protein and 100 times more [32P]-ATP. Also required was a high definition phosphorimager scan of the phosphorylated chip. This required using a high sensitivity phosphor screen and a new high sensitivity scanning instrument recently purchased by our department. After the 4 standardization assays were done, we performed a final assay to obtain the best phosphorylated Ser peptide chip we could produce. A good phosphorylated chip should clearly distinguish each phosphorylated peptide triplet so that the identity of the peptide can unambiguously be assigned. Identifying the phosphorylated peptides was carried out by the company that manufactures the chips and 63 peptides phosphorylated by Adi3 were identified. Using the sequence information for these 63 peptides phosphorylated by Adi3 we can make some estimates about what amino acid are needed for Adi3 to recognize a phosphorylation site. The results showed there was preference in the peptide substrates to contain aromatic hydrophobic residues such as Tryptophan and Tyrosine. Additionally, Aspartic Acid and Arginine appear to be favored in the +4 position and Methionine in the -4 position of the phosphorylated peptides. Finally, the sequence of the 63 identified peptides phosphorylated by Adi3 was used to identify tomato proteins with similar sequences to these peptides. Each peptide sequence was BLASTed against the tomato gene and protein databases. The results returned 1,068 proteins that contained at least 5 amino acids, including the phosphorylatable Ser, identical to any given peptide phosphorylated by Adi3. The highest match of a peptide sequence to a tomato protein was 10 amino acids, which was found for 5 different peptides. Most peptides matched 6 to 8 amino acids in the identified tomato proteins. This list of proteins was further narrowed down to 413 proteins as possible candidates for followup studies based on predicted nuclear localization or relevance to pathogen resistance. This list of 413 proteins was further narrowed to a list of the top 10 proteins. The cDNA for each of these candidates were cloned and analyzed for phosphorylation by Adi3. Three of these candidates showed potential phosphorylation by Adi3. In the previous reporting period we have shown that the protein threonine deaminase 2 (TD2) is dephosphorylated in response to P. syringae flagellin during the basal resistance response to P. syringae in tomato. The deamination of threonine by TD2 to form alpha-ketobutyrate has been shown to be the rate limiting step in the production of isoleucine (Ile). This Ile can then be used for conjugation to the defense hormone jasmonic acid (JA) to generate the active form of jasmonic acid (JA-Ile) for defense against insect herbivores, but JA-Ile has negative effects on resistance to biotrophs such as P. syringae. Thus, we predict that dephosphorylation of TD2 in response to P. syringae flagellin inactivates TD2 in order to reduce JA-Ile. A role for TD2 in the tomato defense response against P. syringae has not yet been shown and our discovery of a potential involvement of TD2 in the basal defense response to P. syringae flagellin opens an exciting new area of research. In the current reporting period we were able to confirm that TD2 is dephosphorylated in response to P. syringae flagellin using phosphatase inhibitors and TD2 specific and TD2 phosphospecific antibodies. This analysis showed that TD2 is dephosphorylated in response to P. syringae flagellin within in 5 minutes. This is followed by a slow recovery of phosphorylation and full recovery by 24 hours after flagellin treatment. This suggests that TD2 is quickly deactivated in response to flagellin. We also cloned the TD2 cDNA into E. coli expression vectors, and successfully purified TD2 protein to assess the role of TD2 dephosphorylation in TD2 functional assays.

Publications

• Type: Journal Articles Status: Published Year Published: 2016 Citation: Miao M, Niu X, Kud J, Du X, Avila J, Devarenne TP, Kuhl J, Liu Y, Xiao F. (2016) The ubiquitin ligase SEVEN IN ABSENTIA (SINA) ubiquitinates a defense-related NAC transcription factor and is involved in defense signaling. New Phytologist. 211:138-148.
• Type: Conference Papers and Presentations Status: Published Year Published: 2016 Citation: Su D and Devarenne TP (2016) Tomato SnRK1 complex functions in pathogen resistance. Abstract for Plant Biology 2016, annual meeting of the American Society of Plant Biologists, Austin, TX. July, 2016.
• Type: Conference Papers and Presentations Status: Published Year Published: 2016 Citation: Yeo I-C and Devarenne TP (2016) Screening for nuclear substrates of the tomato protein kinase Adi3, a cell death suppressor, using a peptide microarray approach. Abstract for Plant Biology 2016, annual meeting of the American Society of Plant Biologists, Austin, TX. July, 2016.
• Type: Conference Papers and Presentations Status: Published Year Published: 2016 Citation: Yeo I-C and Devarenne TP (2016) Functional role of threonine deaminase 2 in the PAMP response of tomato during defense against bacterial infection. Abstract for Plant Biology 2016, annual meeting of the American Society of Plant Biologists, Austin, TX. July, 2016.

Progress 12/15/14 to 12/14/15

Outputs
Target Audience:- The research community studying the interaction of Pseudomonas syringae and other bacteria with plants. - Scientists that are breeding plants for increased resistance to pathogens. Changes/Problems:There have been no changes or problems at this time. What opportunities for training and professional development has the project provided? Funding from this grant has so far allowed for training of two graduate students, Incheol Yeo and Dongyin Su. These students are trained in molecular biology and biochemistry techniques to study plant interactions with pathogens. They were also trained in the writing and the publication process for having a scientific study published in an international scientific journal. Additional training includes reviewing manuscripts from scientific journals, creating poster and oral presentations for scientific meetings, developing networking opportunities, and communicating scientific findings to the public. How have the results been disseminated to communities of interest? Over the past year our studies on cell death control and its role in resistance to P. syringae have been disseminated to the general scientific public through the presentation of a two posters at Plant Biology 2015, the annual meeting of the American Society of Plant Biologists, Minneapolis, MN. July, 2015. What do you plan to do during the next reporting period to accomplish the goals? In the next reporting period we plan to extend our preliminary studies on SnRK1 kinase activity in response to Pst. We will utilize the Pst effector protein AvrPto to assess how it affects SnRK1 kinase activity on known substrates such as nitrate reductase. We will also utilize a Pst mutant without the effector proteins AvrPto and/or AvrPotB. Pst single and double mutants for these genes have been obtained for use. The AvrPto and AvrPtoB Pst effectors are the main effectors involved in the Pto/Prf-mediated resistance to Pst. Thus, these studies will allow us to determine if other effectors are needed for controlling SnRK1 activity. We will also continue our new studies on deciphering the role of threonine deaminase (TD) in the basal resistance response to Pst. We will first confirm that TD is the protein we are interested in studying by using an antibody to TD for studies on TD protein phosphorylation in response to Pst. Once that is confirmed we will silence TD in tomato using virus induced gene silencing followed by treatment with Pst to assess the role of TD in resistance. For these studies we will analyze parameters such as reactive oxygen species production, expression of known defense genes, production of the Ile conjugate of jasmonic acid, and bacterial growth on TD silenced plants.

Impacts
What was accomplished under these goals? During the second year of studies for this grant we have continued our studies on the SnRK1 complex in tomato in response to Pseudomonas syringae pv tomato (Pst). SnRK1 is a protein complex that controls cellular metabolism and interacts with Adi3. SnRK1 is a heterotrimer of alpha, beta, and gamma subunits. The alpha subunit has kinase activity, the beta subunits are known to control the cell localization of the SnRK1 complex, and the gamma subunit control complex kinase activity. We have been studying the two alpha subunits, SnKR1.1 and SnRK1.2 and identified the upstream activator of the alpha subunits; SnRK activating kinase (SnAK). We have found that SnAK significantly activates SnRK1.1 kinase activity. However, SnAK only slightly increases SnRK1.2 kinase activity, indicating the two α-subunits may be regulated differently. We have also discovered that SnRK1.2 seems to inhibit SnRK1.1 kinase activity using in vitro kinase assays. We are now trying to analyze how Pst affects these aspects of SnRK1 activity by transiently expressing the Pst effector protein AvrPto in tomato leaves followed by conducting SnRK1 kinase assays on an extract from the leaves. The preliminary results indicate that AvrPto induces a decrease in SnRK1 kinase activity prior to the onset of the hypersensitive response cell death. This would suggest that tomato alters cellular metabolism during the defense response to Pst. Additionally, in the second year of these studies we have pursued a new avenue for deciphering the resistance mechanisms employed by tomato for defense against Pst. In past years we had developed a phosphospecific antibody to detect Adi3 when it is phosphorylated at its activation site, Ser539. Using in vitro assays, this antibody was capable of distinguishing between Ser539 phosphorylated Adi3 (Adi3pS539) and non-phosphorylated Adi3. However, when the antibody was used to detect Adi3pS539 from a tomato leaf protein extract Adi3pS539 was not detected. Instead, a protein of 59 kDa was detected, which is much smaller than the 77 kDa for Adi3. Thus, it appears the Adi3 phosphospecific antibody is detecting a different protein in vivo. Interestingly, when tomato leaf cells are treated with the flg22 peptide from Pst flagellin, which initiates basal defense responses in tomato, the detection of the 59 kDa protein by the Adi3 phosphospecific antibody is decreased to nearly undetectable levels over a 30 minute time course. This suggests that this 59 kDa protein is being dephosphorylated in response to the detection of Pst flagellin and may play a role in basal defenses against Pst. Thus, we set out to identify this 59 kDa protein. This was accomplished by separating tomato leaf proteins by 2D SDS-PAGE, performing a western blot on this gel with the Adi3 phosphospecific antibody, and then carrying out LC-MS on the protein identified by the western blot. This was repeated 4 times and the same protein was identified each time: threonine deaminase (TD). The deamination of threonine by TD to form alpha-ketobutyrate has been shown to be the rate limiting step in the production of isoleucine (Ile). This Ile can then be used for conjugation to the defense hormone jasmonic acid to generate the active form of jasmonic acid for defense against insect herbivores. A role for TD in the tomato defense response against Pst has not yet been shown and our discovery of a potential involvement of TD in the basal defense response to Pst flagellin opens an exciting new area of research. Our future plans include confirming the dephosphorylation of TD in response to Pst flagellin and deciphering the roles of TD in the defense against Pst. For these studies we have obtained a TD antibody from the laboratory of Greg Howe at Michigan State University.

Publications

• Type: Conference Papers and Presentations Status: Published Year Published: 2015 Citation: Su D and Devarenne TP (2015) Function and regulation of the SnRK1 complex in Tomato. Abstract for Plant Biology 2015, annual meeting of the American Society of Plant Biologists, Minneapolis, MN. July, 2015.
• Type: Conference Papers and Presentations Status: Published Year Published: 2015 Citation: Yeo I-C and Devarenne TP (2015) Isolation and characterization of a novel tomato AGC kinase that is dephosphorylated during the response to Pseudomonas syringae. Abstract for Plant Biology 2015, annual meeting of the American Society of Plant Biologists, Minneapolis, MN. July, 2015.

Progress 12/15/13 to 12/14/14

Outputs
Target Audience: - The research community studying the interaction of Pseudomonas syringae and other bacteria with plants. - Scientists that are breeding plants for increased resistance to pathogens. Changes/Problems: There have been no changes or problems at this time. What opportunities for training and professional development has the project provided? Funding from this grant has so far allowed for training of one graduate student, Incheol Yeo, and in the second year will begin further support of a second graduate student, Dongyin Su. These students are trained in molecular biology and biochemistry techniques to study plant interactions with pathogens. They were also trained in the writing and the publication process for having a scientific study published in an international scientific journal. Additional training includes reviewing manuscripts from scientific journals, creating poster and oral presentations for scientific meetings, developing networking opportunities, and communicating scientific findings to the public. How have the results been disseminated to communities of interest? Over the past year our studies on cell death control and its role in resistance to P. syringae have been disseminated to the general scientific public through a publication in PLOS ONE and the presentation of a poster at Plant Biology 2014, the annual meeting of the American Society of Plant Biologists, Portland, OR. July, 2014. What do you plan to do during the next reporting period to accomplish the goals? In the next reporting period we plan to extend our SnRK1/beta subunit interaction and phosphorylation studies to how these events control the cellular localization for the SnRK1 complex. We will start by analyzing the cellular localization in the absence of the Pst pathogen using confocal microscopy with SnRK1 and beta subunits tagged with fluorescent proteins. We will also use subcellular fractionation followed by western blot to back up the confocal microscopy. Once we have defined the cell localization without the pathogen, we will incorporate the expression of the Pst effector protein AvrPto to see how this will alter the SnRK1/beta subunit localization. We also expect within the next reporting period to finalize our phosphoproteomics studies to identify Adi3 controlled nuclear phosphorylation events. These studies are supported by NSF and the use of this data to identify and study Adi3 phosphorylation substrates and their role in PCD control in response to Pst is supported by this USDA grant. Once the NSF studies are finalized we will begin to identify Adi3 phosphorylated proteins to study for the USDA studies. We expect to have several candidates identified and cloned for future studies.

Impacts
What was accomplished under these goals? During the first year of studies for this grant we have concluded and published studies that identified a molecular mechanism by which PCD in tomato is initiated during the defense response to the Pst effector protein AvrPto. In previous studies we determined that Adi3 is localized mainly to the cell nucleus where it suppresses cell death, and that Adi3 travels along the endosomal system from the cell membrane to the nucleus. In the current study we determined that in response to the Pst effector AvrPto, Adi3 is restricted to the endosomal systems and not allowed to enter the nucleus. Thus, Adi3 can no longer suppress cell death and the PCD needed for resistance to Pst is initiated. These studies were recently accepted for publication in PLOS ONE. We have also made progress on understanding how cell localization is controlled for SnRK1, a protein complex that controls cellular metabolism and interacts with Adi3. SnRK1 is a heterotrimer of alpha, beta, and gamma subunits. The beta subunits are known to control the cell localization of the SnRK1 complex and so we have started our studies by analyzing the interaction of the two alpha subunits, SnKR1.1 and SnRK1.2, and the four beta subunits. We have found that while both SnKR1.1 and SnRK1.2 interact with all beta subunits, they preferential interact with the Gal83 and Tau1 beta subunits. Since both SnKR1.1 and SnRK1.2 are kinases, we also analyzed the ability of these kinases to phosphorylate the beta subunits. We found that similar to the interaction studies, both SnKR1.1 and SnRK1.2 phosphorylate Gal83 and Tau1 preferentially. These findings were presented in a poster at Plant Biology 2014 and are now being applied to cellular localization control for the SnRK1 entire complex in response to Pst.

Publications

• Type: Journal Articles Status: Accepted Year Published: 2014 Citation: Ek-Ramos MJ, Avila J, Nelson Dittrich AC, Su D, Gray JW, Devarenne TP (2014). The tomato cell death suppressor Adi3 is restricted to the endosomal system in response to the Pseudomonas syringae effector protein AvrPto. PLOS ONE. In Press.
• Type: Conference Papers and Presentations Status: Accepted Year Published: 2014 Citation: Su D and Devarenne TP (2014) Interactions between the plant cell death suppressor Adi3 and subunits of the metabolism regulating SnKR1 complex. Poster abstract for Plant Biology 2014, annual meeting of the American Society of Plant Biologists, Portland, OR. July, 2014.