Proteomics-based sequence analysis of plant gene expression – the chloroplast transcription apparatus
Database screening helped to identify regulatory proteins of chloroplast RNA polymerase, including a novel putative RNA-binding protein (RBP).The previously identified transcription kinase (cpCK2) is likely to play a common role in number of plant species The chloroplast transcription apparatus has...
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Published in | Phytochemistry (Oxford) Vol. 65; no. 12; pp. 1785 - 1793 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.06.2004
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Subjects | |
Online Access | Get full text |
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Summary: | Database screening helped to identify regulatory proteins of chloroplast RNA polymerase, including a novel putative RNA-binding protein (RBP).The previously identified transcription kinase (cpCK2) is likely to play a common role in number of plant species
The chloroplast transcription apparatus has turned out to be more complex than anticipated, with core polypeptides surrounded by multiple accessory proteins of diverse, and in part unexpected, functions. At least two different RNA-binding proteins and several redox-responsive proteins are components of the major chloroplast RNA polymerase termed PEP-A. One of the key-regulatory factors has been identified as a Ser/Thr-specific protein kinase that is sensitive to SH group modification by glutathione and by this means is able to modulate transcription. The cloned plastid transcription kinase from mustard (Sinapis alba L.) has been assigned as a member of the (mostly nucleo-cytosolic) CK2 family and hence has been termed cpCK2. Despite its apparent role in mustard chloroplast transcription, until recently no data have been available for other plant species. Using the web database resources, we find evidence for an evolutionarily conserved role of this redox-sensitive plastid transcription factor. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0031-9422 1873-3700 |
DOI: | 10.1016/j.phytochem.2004.04.034 |