PTK, the chloroplast RNA polymerase-associated protein kinase from mustard (Sinapis alba), mediates redox control of plastid in vitro transcription

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Authors

  • S Baginsky
  • K Tiller
  • T Pfannschmidt
  • G Link

Research Organisations

External Research Organisations

  • Bochum University of Applied Sciences
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Details

Original languageEnglish
Pages (from-to)1013-23
Number of pages11
JournalPlant molecular biology
Volume39
Issue number5
Publication statusPublished - Mar 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.

Keywords

    Chloroplasts/drug effects, DNA-Directed RNA Polymerases/metabolism, Glutathione/pharmacology, Mustard Plant/drug effects, Oxidation-Reduction, Peptides/metabolism, Photosynthetic Reaction Center Complex Proteins/genetics, Photosystem II Protein Complex, Plants, Medicinal, Promoter Regions, Genetic, Protein-Serine-Threonine Kinases/metabolism, Substrate Specificity, Transcription, Genetic

Cite this

PTK, the chloroplast RNA polymerase-associated protein kinase from mustard (Sinapis alba), mediates redox control of plastid in vitro transcription. / Baginsky, S; Tiller, K; Pfannschmidt, T et al.
In: Plant molecular biology, Vol. 39, No. 5, 03.1999, p. 1013-23.

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title = "PTK, the chloroplast RNA polymerase-associated protein kinase from mustard (Sinapis alba), mediates redox control of plastid in vitro transcription",
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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author = "S Baginsky and K Tiller and T Pfannschmidt and G Link",
note = "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.",
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Download

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 -