Proteomics-based sequence analysis of plant gene expression--the chloroplast transcription apparatus

Phytochemistry. 2004 Jun;65(12):1785-93. doi: 10.1016/j.phytochem.2004.04.034.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Chloroplasts / genetics*
  • Chloroplasts / metabolism
  • DNA-Directed RNA Polymerases / analysis
  • DNA-Directed RNA Polymerases / isolation & purification
  • Databases, Protein
  • Gene Expression*
  • Molecular Sequence Data
  • Molecular Weight
  • Mustard Plant / genetics*
  • Mustard Plant / metabolism
  • Plant Proteins / analysis
  • Plant Proteins / isolation & purification
  • Protein-Serine-Threonine Kinases / analysis
  • Proteomics*
  • RNA-Binding Proteins / analysis
  • RNA-Binding Proteins / isolation & purification
  • Sequence Analysis / methods*
  • Sequence Homology, Amino Acid
  • Transcription, Genetic*


  • Plant Proteins
  • RNA-Binding Proteins
  • Protein-Serine-Threonine Kinases
  • DNA-Directed RNA Polymerases