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Conservation between higher plants and the moss Physcomitrella patens in response to the phytohormone abscisic acid: a proteomics analysis.

ABSTRACT: BACKGROUND: The plant hormone abscisic acid (ABA) is ubiquitous among land plants where it plays an important role in plant growth and development. In seeds, ABA induces embryogenesis and seed maturation as well as seed dormancy and germination. In vegetative tissues, ABA is a necessary mediator in the triggering of many of the physiological and molecular adaptive responses of the plant to adverse environmental conditions, such as desiccation, salt and cold. RESULTS: In this study, we investigated the influence of abscisic acid (ABA) on Physcomitrella patens at the level of the proteome using two-dimensional gel electrophoresis (2-DE) and liquid chromatography-tandem mass spectrometry (LC-MS/MS). Sixty-five protein spots showed changes in response to ABA treatment. Among them, thirteen protein spots were down-regulated; fifty-two protein spots were up-regulated including four protein spots which were newly induced. These proteins were involved in various functions, including material and energy metabolism, defense, protein destination and storage, transcription, signal transduction, cell growth/division, transport, and cytoskeleton. Specifically, most of the up-regulated proteins functioned as molecular chaperones, transcriptional regulators, and defense proteins. Detailed analysis of these up-regulated proteins showed that ABA could trigger stress and defense responses and protect plants from oxidative damage. Otherwise, three protein kinases involved in signal pathways were up-regulated suggesting that P. patens is sensitive to exogenous ABA. The down-regulated of the Rubisco small subunit, photosystem II oxygen-evolving complex proteins and photosystem assembly protein ycf3 indicated that photosynthesis of P. patens was inhibited by ABA treatment. CONCLUSION: Proteome analysis techniques have been applied as a direct, effective, and reliable tool in differential protein expressions. Sixty-five protein spots showed differences in accumulation levels as a result of treatment with ABA. Detailed analysis these protein functions showed that physiological and molecular responses to the plant hormone ABA appear to be conserved among higher plant species and bryophytes.

SUBMITTER: Wang X

PROVIDER: S-EPMC2956542 | biostudies-literature | 2010

REPOSITORIES: biostudies-literature

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Conservation between higher plants and the moss Physcomitrella patens in response to the phytohormone abscisic acid: a proteomics analysis.

Wang Xiaoqin X Kuang Tingyun T He Yikun Y

BMC plant biology 20100827

<h4>Background</h4>The plant hormone abscisic acid (ABA) is ubiquitous among land plants where it plays an important role in plant growth and development. In seeds, ABA induces embryogenesis and seed maturation as well as seed dormancy and germination. In vegetative tissues, ABA is a necessary mediator in the triggering of many of the physiological and molecular adaptive responses of the plant to adverse environmental conditions, such as desiccation, salt and cold.<h4>Results</h4>In this study, ...[more]

PMID: 20799958

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Project description:BACKGROUND: Hexokinase catalyzes the phosphorylation of glucose and fructose, but it is also involved in sugar sensing in both fungi and plants. We have previously described two types of hexokinases in the moss Physcomitrella. Type A, exemplified by PpHxk1, the major hexokinase in Physcomitrella, is a soluble protein that localizes to the chloroplast stroma. Type B, exemplified by PpHxk2, has an N-terminal membrane anchor. Both types are found also in vascular plants, and localize to the chloroplast stroma and mitochondrial membranes, respectively. RESULTS: We have now characterized all 11 hexokinase encoding genes in Physcomitrella. Based on their N-terminal sequences and intracellular localizations, three of the encoded proteins are type A hexokinases and four are type B hexokinases. One of the type B hexokinases has a splice variant without a membrane anchor, that localizes to the cytosol and the nucleus. However, we also found two new types of hexokinases with no obvious orthologs in vascular plants. Type C, encoded by a single gene, has neither transit peptide nor membrane anchor, and is found in the cytosol and in the nucleus. Type D hexokinases, encoded by three genes, have membrane anchors and localize to mitochondrial membranes, but their sequences differ from those of the type B hexokinases. Interestingly, all moss hexokinases are more similar to each other in overall sequence than to hexokinases from other plants, even though characteristic sequence motifs such as the membrane anchor of the type B hexokinases are highly conserved between moss and vascular plants, indicating a common origin for hexokinases of the same type. CONCLUSIONS: We conclude that the hexokinase gene family is more diverse in Physcomitrella, encoding two additional types of hexokinases that are absent in vascular plants. In particular, the presence of a cytosolic and nuclear hexokinase (type C) sets Physcomitrella apart from vascular plants, and instead resembles yeast, where all hexokinases localize to the cytosol. The fact that all moss hexokinases are more similar to each other than to hexokinases from vascular plants, even though both type A and type B hexokinases are present in all plants, further suggests that the hexokinase gene family in Physcomitrella has undergone concerted evolution.

Dataset Information

Conservation between higher plants and the moss Physcomitrella patens in response to the phytohormone abscisic acid: a proteomics analysis.

Publications

Conservation between higher plants and the moss Physcomitrella patens in response to the phytohormone abscisic acid: a proteomics analysis.

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