Details
| Original language | English |
|---|---|
| Pages (from-to) | 253-61 |
| Number of pages | 9 |
| Journal | European Journal of Biochemistry |
| Volume | 267 |
| Issue number | 1 |
| Publication status | Published - Jan 2000 |
| Externally published | Yes |
Abstract
We previously identified two multisubunit plastid RNA polymerases termed A and B. The B enzyme has a bacterial-type polypeptide composition and is sensitive to the prokaryotic transcription inhibitor rifampicin (Rif); the A enzyme has a more complex subunit structure and is Rif-resistant. Here we report results of N-terminal sequencing and MS carried out with the A enzyme, which establish that the latter contains rpo gene products and is structurally related to the B enzyme. Furthermore, evidence is provided that the A enzyme can be converted into a Rif-sensitive enzyme form in a phosphorylation-dependent manner in vitro by a treatment that results in depletion of a beta-like subunit. Database searches using sequence information derived from additional polypeptides that are present in purified A preparations revealed sequence similarity with chloroplast proteins involved in RNA processing and redox control. This proteomics approach thus points to the complexity of the chloroplast transcription apparatus and its interconnections with post-transcriptional and signalling mechanisms.
Keywords
- Alkaline Phosphatase/metabolism, Amino Acid Sequence, Chloroplasts/enzymology, Cyclic AMP-Dependent Protein Kinases/metabolism, Genes, Plant/genetics, Molecular Sequence Data, Molecular Weight, Mustard Plant/cytology, Peptides/chemistry, Phosphorylation, Plants, Medicinal, RNA Polymerase I/antagonists & inhibitors, RNA Polymerase II/chemistry, Rifampin/pharmacology, Sequence Alignment, Sequence Analysis, Protein, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Superoxide Dismutase/chemistry
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In: European Journal of Biochemistry, Vol. 267, No. 1, 01.2000, p. 253-61.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - The multisubunit chloroplast RNA polymerase A from mustard (Sinapis alba L.). Integration of a prokaryotic core into a larger complex with organelle-specific functions
AU - Pfannschmidt, T
AU - Ogrzewalla, K
AU - Baginsky, S
AU - Sickmann, A
AU - Meyer, H E
AU - Link, G
PY - 2000/1
Y1 - 2000/1
N2 - We previously identified two multisubunit plastid RNA polymerases termed A and B. The B enzyme has a bacterial-type polypeptide composition and is sensitive to the prokaryotic transcription inhibitor rifampicin (Rif); the A enzyme has a more complex subunit structure and is Rif-resistant. Here we report results of N-terminal sequencing and MS carried out with the A enzyme, which establish that the latter contains rpo gene products and is structurally related to the B enzyme. Furthermore, evidence is provided that the A enzyme can be converted into a Rif-sensitive enzyme form in a phosphorylation-dependent manner in vitro by a treatment that results in depletion of a beta-like subunit. Database searches using sequence information derived from additional polypeptides that are present in purified A preparations revealed sequence similarity with chloroplast proteins involved in RNA processing and redox control. This proteomics approach thus points to the complexity of the chloroplast transcription apparatus and its interconnections with post-transcriptional and signalling mechanisms.
AB - We previously identified two multisubunit plastid RNA polymerases termed A and B. The B enzyme has a bacterial-type polypeptide composition and is sensitive to the prokaryotic transcription inhibitor rifampicin (Rif); the A enzyme has a more complex subunit structure and is Rif-resistant. Here we report results of N-terminal sequencing and MS carried out with the A enzyme, which establish that the latter contains rpo gene products and is structurally related to the B enzyme. Furthermore, evidence is provided that the A enzyme can be converted into a Rif-sensitive enzyme form in a phosphorylation-dependent manner in vitro by a treatment that results in depletion of a beta-like subunit. Database searches using sequence information derived from additional polypeptides that are present in purified A preparations revealed sequence similarity with chloroplast proteins involved in RNA processing and redox control. This proteomics approach thus points to the complexity of the chloroplast transcription apparatus and its interconnections with post-transcriptional and signalling mechanisms.
KW - Alkaline Phosphatase/metabolism
KW - Amino Acid Sequence
KW - Chloroplasts/enzymology
KW - Cyclic AMP-Dependent Protein Kinases/metabolism
KW - Genes, Plant/genetics
KW - Molecular Sequence Data
KW - Molecular Weight
KW - Mustard Plant/cytology
KW - Peptides/chemistry
KW - Phosphorylation
KW - Plants, Medicinal
KW - RNA Polymerase I/antagonists & inhibitors
KW - RNA Polymerase II/chemistry
KW - Rifampin/pharmacology
KW - Sequence Alignment
KW - Sequence Analysis, Protein
KW - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
KW - Superoxide Dismutase/chemistry
U2 - 10.1046/j.1432-1327.2000.00991.x
DO - 10.1046/j.1432-1327.2000.00991.x
M3 - Article
C2 - 10601874
VL - 267
SP - 253
EP - 261
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
SN - 0014-2956
IS - 1
ER -