Transcription factor phosphorylation by a protein kinase associated with chloroplast RNA polymerase from mustard (Sinapis alba)

Transcription factor phosphorylation by a protein kinase associated with chloroplast RNA... The chloroplast transcription machinery involves multiple components with both catalytic and regulatory functions. Here we describe a serine-specific protein kinase activity that is associated with the major chloroplast RNA polymerase and phosphorylates sigma-like transcription factors in vitro. The kinase activity can be assigned to a 54 kDa polypeptide of partially purified RNA polymerase (KPC, kinase polymerase complex). This polypeptide is also present in a smaller complex that contains several putative polymerase subunits and reveals kinase activity but lacks transcription activity (KC, kinase complex). Although the 54 kDa component could not be chromatographically separated from the rest of this complex without loss of activity, it retained residual kinase activity in an electrophoretic blot assay. The polymerase-associated kinase is itself affected by in vitro phosphorylation and dephosphorylation, which raises the possibility that it is part of a signalling cascade that controls chloroplast transcription in vivo by factor phosphorylation. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Transcription factor phosphorylation by a protein kinase associated with chloroplast RNA polymerase from mustard (Sinapis alba)

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 1997 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1005802909902
Publisher site
See Article on Publisher Site

Abstract

The chloroplast transcription machinery involves multiple components with both catalytic and regulatory functions. Here we describe a serine-specific protein kinase activity that is associated with the major chloroplast RNA polymerase and phosphorylates sigma-like transcription factors in vitro. The kinase activity can be assigned to a 54 kDa polypeptide of partially purified RNA polymerase (KPC, kinase polymerase complex). This polypeptide is also present in a smaller complex that contains several putative polymerase subunits and reveals kinase activity but lacks transcription activity (KC, kinase complex). Although the 54 kDa component could not be chromatographically separated from the rest of this complex without loss of activity, it retained residual kinase activity in an electrophoretic blot assay. The polymerase-associated kinase is itself affected by in vitro phosphorylation and dephosphorylation, which raises the possibility that it is part of a signalling cascade that controls chloroplast transcription in vivo by factor phosphorylation.

Journal

Plant Molecular BiologySpringer Journals

Published: Sep 29, 2004

References

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