Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 1013-23 |
| Seitenumfang | 11 |
| Fachzeitschrift | Plant molecular biology |
| Jahrgang | 39 |
| Ausgabenummer | 5 |
| Publikationsstatus | Veröffentlicht - März 1999 |
Abstract
The major RNA polymerase from mustard chloroplasts is a multi-subunit enzyme consisting of core components and associated factors. Among the latter is a heterotrimeric factor named PTK (plastid transcription kinase) because of its serine/threonine-type protein kinase activity. PTK activity itself depends on its phosphorylation state. In addition, we show that it responds to glutathione but not to other redox-reactive reagents that were tested, and both glutathione and phosphorylation act antagonistically. Using a homologous in vitro system, we find that PTK selectively phosphorylates subunit(s) of plastid RNA polymerase and is involved in determining the level of faithful transcription from the chloroplast psbA promoter. Together, these results establish a role for phosphorylation and redox state in the regulation of plastid gene expression.
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in: Plant molecular biology, Jahrgang 39, Nr. 5, 03.1999, S. 1013-23.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - PTK, the chloroplast RNA polymerase-associated protein kinase from mustard (Sinapis alba), mediates redox control of plastid in vitro transcription
AU - Baginsky, S
AU - Tiller, K
AU - Pfannschmidt, T
AU - Link, G
N1 - Funding information: We thank Claudia Wittig for technical assistance. This work was supported by the Deutsche Forschungsge-meinschaft (Li 261/14-2) and the Fonds der Chemis-chen Industrie, Germany.
PY - 1999/3
Y1 - 1999/3
N2 - The major RNA polymerase from mustard chloroplasts is a multi-subunit enzyme consisting of core components and associated factors. Among the latter is a heterotrimeric factor named PTK (plastid transcription kinase) because of its serine/threonine-type protein kinase activity. PTK activity itself depends on its phosphorylation state. In addition, we show that it responds to glutathione but not to other redox-reactive reagents that were tested, and both glutathione and phosphorylation act antagonistically. Using a homologous in vitro system, we find that PTK selectively phosphorylates subunit(s) of plastid RNA polymerase and is involved in determining the level of faithful transcription from the chloroplast psbA promoter. Together, these results establish a role for phosphorylation and redox state in the regulation of plastid gene expression.
AB - The major RNA polymerase from mustard chloroplasts is a multi-subunit enzyme consisting of core components and associated factors. Among the latter is a heterotrimeric factor named PTK (plastid transcription kinase) because of its serine/threonine-type protein kinase activity. PTK activity itself depends on its phosphorylation state. In addition, we show that it responds to glutathione but not to other redox-reactive reagents that were tested, and both glutathione and phosphorylation act antagonistically. Using a homologous in vitro system, we find that PTK selectively phosphorylates subunit(s) of plastid RNA polymerase and is involved in determining the level of faithful transcription from the chloroplast psbA promoter. Together, these results establish a role for phosphorylation and redox state in the regulation of plastid gene expression.
KW - Chloroplasts/drug effects
KW - DNA-Directed RNA Polymerases/metabolism
KW - Glutathione/pharmacology
KW - Mustard Plant/drug effects
KW - Oxidation-Reduction
KW - Peptides/metabolism
KW - Photosynthetic Reaction Center Complex Proteins/genetics
KW - Photosystem II Protein Complex
KW - Plants, Medicinal
KW - Promoter Regions, Genetic
KW - Protein-Serine-Threonine Kinases/metabolism
KW - Substrate Specificity
KW - Transcription, Genetic
U2 - 10.1023/a:1006177807844
DO - 10.1023/a:1006177807844
M3 - Article
C2 - 10344206
VL - 39
SP - 1013
EP - 1023
JO - Plant molecular biology
JF - Plant molecular biology
SN - 0167-4412
IS - 5
ER -