Details
| Original language | English |
|---|---|
| Pages (from-to) | 1043-55 |
| Number of pages | 13 |
| Journal | Plant physiology |
| Volume | 157 |
| Issue number | 3 |
| Publication status | Published - Nov 2011 |
Abstract
The major RNA polymerase activity in mature chloroplasts is a multisubunit, Escherichia coli-like protein complex called PEP (for plastid-encoded RNA polymerase). Its subunit structure has been extensively investigated by biochemical means. Beside the "prokaryotic" subunits encoded by the plastome-located RNA polymerase genes, a number of additional nucleus-encoded subunits of eukaryotic origin have been identified in the PEP complex. These subunits appear to provide additional functions and regulation modes necessary to adapt transcription to the varying functional situations in chloroplasts. However, despite the enormous progress in genomic data and mass spectrometry techniques, it is still under debate which of these subunits belong to the core complex of PEP and which ones represent rather transient or peripheral components. Here, we present a catalog of true PEP subunits that is based on comparative analyses from biochemical purifications, protein mass spectrometry, and phenotypic analyses. We regard reproducibly identified protein subunits of the basic PEP complex as essential when the corresponding knockout mutants reveal an albino or pale-green phenotype. Our study provides a clearly defined subunit catalog of the basic PEP complex, generating the basis for a better understanding of chloroplast transcription regulation. In addition, the data support a model that links PEP complex assembly and chloroplast buildup during early seedling development in vascular plants.
Keywords
- Amino Acid Sequence, Arabidopsis/enzymology, DNA-Directed RNA Polymerases/chemistry, Electrophoresis, Gel, Two-Dimensional, Gene Knockout Techniques, Homozygote, Models, Biological, Molecular Sequence Data, Mustard Plant/enzymology, Mutation/genetics, Phenotype, Plastids/enzymology, Protein Subunits/chemistry, Spectrometry, Mass, Electrospray Ionization
Cite this
- Standard
- Harvard
- Apa
- Vancouver
- BibTeX
- RIS
In: Plant physiology, Vol. 157, No. 3, 11.2011, p. 1043-55.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Identification of essential subunits in the plastid-encoded RNA polymerase complex reveals building blocks for proper plastid development
AU - Steiner, Sebastian
AU - Schröter, Yvonne
AU - Pfalz, Jeannette
AU - Pfannschmidt, Thomas
PY - 2011/11
Y1 - 2011/11
N2 - The major RNA polymerase activity in mature chloroplasts is a multisubunit, Escherichia coli-like protein complex called PEP (for plastid-encoded RNA polymerase). Its subunit structure has been extensively investigated by biochemical means. Beside the "prokaryotic" subunits encoded by the plastome-located RNA polymerase genes, a number of additional nucleus-encoded subunits of eukaryotic origin have been identified in the PEP complex. These subunits appear to provide additional functions and regulation modes necessary to adapt transcription to the varying functional situations in chloroplasts. However, despite the enormous progress in genomic data and mass spectrometry techniques, it is still under debate which of these subunits belong to the core complex of PEP and which ones represent rather transient or peripheral components. Here, we present a catalog of true PEP subunits that is based on comparative analyses from biochemical purifications, protein mass spectrometry, and phenotypic analyses. We regard reproducibly identified protein subunits of the basic PEP complex as essential when the corresponding knockout mutants reveal an albino or pale-green phenotype. Our study provides a clearly defined subunit catalog of the basic PEP complex, generating the basis for a better understanding of chloroplast transcription regulation. In addition, the data support a model that links PEP complex assembly and chloroplast buildup during early seedling development in vascular plants.
AB - The major RNA polymerase activity in mature chloroplasts is a multisubunit, Escherichia coli-like protein complex called PEP (for plastid-encoded RNA polymerase). Its subunit structure has been extensively investigated by biochemical means. Beside the "prokaryotic" subunits encoded by the plastome-located RNA polymerase genes, a number of additional nucleus-encoded subunits of eukaryotic origin have been identified in the PEP complex. These subunits appear to provide additional functions and regulation modes necessary to adapt transcription to the varying functional situations in chloroplasts. However, despite the enormous progress in genomic data and mass spectrometry techniques, it is still under debate which of these subunits belong to the core complex of PEP and which ones represent rather transient or peripheral components. Here, we present a catalog of true PEP subunits that is based on comparative analyses from biochemical purifications, protein mass spectrometry, and phenotypic analyses. We regard reproducibly identified protein subunits of the basic PEP complex as essential when the corresponding knockout mutants reveal an albino or pale-green phenotype. Our study provides a clearly defined subunit catalog of the basic PEP complex, generating the basis for a better understanding of chloroplast transcription regulation. In addition, the data support a model that links PEP complex assembly and chloroplast buildup during early seedling development in vascular plants.
KW - Amino Acid Sequence
KW - Arabidopsis/enzymology
KW - DNA-Directed RNA Polymerases/chemistry
KW - Electrophoresis, Gel, Two-Dimensional
KW - Gene Knockout Techniques
KW - Homozygote
KW - Models, Biological
KW - Molecular Sequence Data
KW - Mustard Plant/enzymology
KW - Mutation/genetics
KW - Phenotype
KW - Plastids/enzymology
KW - Protein Subunits/chemistry
KW - Spectrometry, Mass, Electrospray Ionization
U2 - 10.1104/pp.111.184515
DO - 10.1104/pp.111.184515
M3 - Article
C2 - 21949211
VL - 157
SP - 1043
EP - 1055
JO - Plant physiology
JF - Plant physiology
SN - 0032-0889
IS - 3
ER -