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Similar but not identical – a quadruple pack of LSU (RESPONSE TO LOW SULFUR) from Arabidopsis thaliana

ABSTRACT: The members of plant-specific LSU (RESPONSE TO LOW SULFUR) family were first identified as strongly induced during sulfur starvation. Molecular function of these protein remains unknown, however they were identified as important stress-related hubs by several research groups. In Arabidopsis thaliana there are four members of LSU family. These proteins are involved in multiple protein-protein interactions and literature data suggest that they can integrate abiotic and biotic stress responses. LSU proteins are small and have the coiled-coil structure. Additionally to binding with other proteins they can form homo- and heterodimers and possibly also multimers. In this work we investigated interactions between different monomers of LSU1-4 using Y2H and BiFC methods. The differences in strength of various homo- and heterodimers formation were observed. The constructed by us structural models of the LSU1-4 homo- and heterodimers were in agreement with the experimental observations concerning differences in strength of dimers formation and might help understanding interaction of LSU with other partners. Since previously the partners of LSU were identified using the Y2H approach we decided to obtain the lists of LSU interactors in plants using the TAP-tagged LSU1-4. Interaction of LSUs with a few selected proteins from the lists was verified by Y2H and BiFC.

INSTRUMENT(S): LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

SUBMITTER: Dominik Cysewski

LAB HEAD: Agnieszka Sirko

PROVIDER: PXD016023 | Pride | 2020-08-12

REPOSITORIES: Pride

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Project description:Autophagy involvement in plant response to nitrogen, carbon and sulfur starvation was already reported, however the mechanisms responsible for its regulation and selectivity in such conditions were not yet investigated. We observed increased amounts of NBR1 transcript in plants exposed to sulfur deficit as compared to the control plants grown in nutrient sufficient conditions. This observation prompted us to investigate the role of this selective autophagy cargo receptor in plant response to sulfur deficit. Transcriptome analysis of the wild type and NBR overexpressing plants revealed differences in gene expression changes in response to sulfur deficit. Moreover, NBR1 overexpressors have significantly shorter roots than WT, when grown in nutrient deficient conditions in the presence of TOR kinase inhibitors, namely in the conditions leading to autophagy induction. Besides, NBR1 overexpression promoted stomata closure while NBR1 depletion stomata opening. Surprisingly, all lines had more closed stomata when grown in sulfur deficient than sulfur optimal conditions, what indicates that this effect is independent from NBR1. Similarly, ABA-dependent stomatal closure was independent from NBR1 and growth conditions. Cysteine also promoted stomatal closure in NBR1-independent way in plants grown in the optimal medium but in contrast, reduced the number of open stomata in plants from sulfur deficient medium. Interaction network analysis of the proteins co-purifying with NBR1 revealed links with proteins involved in degradation systems, and endosomal trafficking and a surprizing connection with nuclear transport. In addition, several proteins co-purifying with NBR1 were found only in sulfur deficient conditions. One of them, ribosomal protein S6 (RPS6) was further confirmed as a direct NBR1 interactor. Localization of the RPS6 interaction sites in NBR1 indicated that ubiquitin binding domain of NBR1 is not required for this interaction what means that it is rather not the classical “ubiquitinated target - autophagy receptor” interaction.

Project description:Boehm2014 - isoform-specific dimerization of pSTAT5A and pSTAT5B To study STAT5 activation, the authors build a dynamic model of pSTAT5 isoform dimerization. Combinatorial binding of pSTAT5A and pSTAT5B is analysed using model hypotheses and concurrent experiments. Model parameters are derived from the experiments on Ba/F3 cells. Results show that pSTAT5 heterodimerization hypothesis for STAT5 activation favours experimental results. This model is described in the article: Identification of isoform-specific dynamics in phosphorylation-dependent STAT5 dimerization by quantitative mass spectrometry and mathematical modeling Boehm ME, Adlung L, Schilling M, Roth S, Klingmüller U, Lehmann WD J Proteome Res. 2014 Dec 5;13(12):5685-94 Abstract: STAT5A and STAT5B are important transcription factors that dimerize and transduce activation signals of cytokine receptors directly to the nucleus. A typical cytokine that mediates STAT5 activation is erythropoietin (Epo). Differential functions of STAT5A and STAT5B have been reported. However, the extent to which phosphorylated STAT5A and STAT5B (pSTAT5A, pSTAT5B) form homo- or heterodimers is not understood, nor is how this might influence the signal transmission to the nucleus. To study this, we designed a concept to investigate the isoform-specific dimerization behavior of pSTAT5A and pSTAT5B that comprises isoform-specific immunoprecipitation (IP), measurement of the degree of phosphorylation, and isoform ratio determination between STAT5A and STAT5B. For the main analytical method, we employed quantitative label-free and -based mass spectrometry. For the cellular model system, we used Epo receptor (EpoR)-expressing BaF3 cells (BaF3-EpoR) stimulated with Epo. Three hypotheses of dimer formation between pSTAT5A and pSTAT5B were used to explain the analytical results by a static mathematical model: formation of (i) homodimers only, (ii) heterodimers only, and (iii) random formation of homo- and heterodimers. The best agreement between experimental data and model simulations was found for the last case. Dynamics of cytoplasmic STAT5 dimerization could be explained by distinct nuclear import rates and individual nuclear retention for homo- and heterodimers of phosphorylated STAT5. This model is hosted on BioModels Database and identified by: BIOMD0000000591. To cite BioModels Database, please use: BioModels: Content, Features, Functionality, and Use.. To the extent possible under law, all copyright and related or neighbouring rights to this encoded model have been dedicated to the public domain worldwide. Please refer to CC0 Public Domain Dedication for more information.

			Action	DRS
	70408niemi_A.raw	Raw
	70408niemi_AA.raw	Raw
	70408niemi_B.raw	Raw
	70408niemi_BB.raw	Raw
	70408niemi_C.raw	Raw

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Similar but not identical – a quadruple pack of LSU (RESPONSE TO LOW SULFUR) from Arabidopsis thaliana

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