A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana

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A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana. / Schliebner, I; Pribil, M; Zühlke, J; Dietzmann, A; Leister, D.

In: Current Genomics, Vol. 9, No. 3, 2008, p. 184-90.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Schliebner, I, Pribil, M, Zühlke, J, Dietzmann, A & Leister, D 2008, 'A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana', Current Genomics, vol. 9, no. 3, pp. 184-90. https://doi.org/10.2174/138920208784340740

APA

Schliebner, I., Pribil, M., Zühlke, J., Dietzmann, A., & Leister, D. (2008). A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana. Current Genomics, 9(3), 184-90. https://doi.org/10.2174/138920208784340740

Vancouver

Schliebner I, Pribil M, Zühlke J, Dietzmann A, Leister D. A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana. Current Genomics. 2008;9(3):184-90. https://doi.org/10.2174/138920208784340740

Author

Schliebner, I ; Pribil, M ; Zühlke, J ; Dietzmann, A ; Leister, D. / A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana. In: Current Genomics. 2008 ; Vol. 9, No. 3. pp. 184-90.

Bibtex

@article{d272a5fc5d284ebc8170b3e767b82b54,
title = "A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana",
abstract = "Protein phosphorylation is a major mode of regulation of metabolism, gene expression and cell architecture. In chloroplasts, reversible phosphorylation of proteins is known to regulate a number of prominent processes, for instance photosynthesis, gene expression and starch metabolism. The complements of the involved chloroplast protein kinases (cpPKs) and phosphatases (cpPPs) are largely unknown, except 6 proteins (4 cpPKs and 2 cpPPs) which have been experimentally identified so far. We employed combinations of programs predicting N-terminal chloroplast transit peptides (cTPs) to identify 45 tentative cpPKs and 21 tentative cpPPs. However, test sets of 9 tentative cpPKs and 13 tentative cpPPs contain only 2 and 7 genuine cpPKs and cpPPs, respectively, based on experimental subcellular localization of their N-termini fused to the reporter protein RFP. Taken together, the set of enzymes known to be involved in the reversible phosphorylation of chloroplast proteins in A. thaliana comprises altogether now 6 cpPKs and 9 cpPPs, the function of which needs to be determined in future by functional genomics approaches. This includes the calcium-regulated PK CIPK13 which we found to be located in the chloroplast, indicating that calcium-dependent signal transduction pathways also operate in this organelle.",
keywords = "Journal Article",
author = "I Schliebner and M Pribil and J Z{\"u}hlke and A Dietzmann and D Leister",
year = "2008",
doi = "10.2174/138920208784340740",
language = "English",
volume = "9",
pages = "184--90",
journal = "Current Genomics",
issn = "1389-2029",
publisher = "Bentham Science Publishers",
number = "3",

}

RIS

TY - JOUR

T1 - A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana

AU - Schliebner, I

AU - Pribil, M

AU - Zühlke, J

AU - Dietzmann, A

AU - Leister, D

PY - 2008

Y1 - 2008

N2 - Protein phosphorylation is a major mode of regulation of metabolism, gene expression and cell architecture. In chloroplasts, reversible phosphorylation of proteins is known to regulate a number of prominent processes, for instance photosynthesis, gene expression and starch metabolism. The complements of the involved chloroplast protein kinases (cpPKs) and phosphatases (cpPPs) are largely unknown, except 6 proteins (4 cpPKs and 2 cpPPs) which have been experimentally identified so far. We employed combinations of programs predicting N-terminal chloroplast transit peptides (cTPs) to identify 45 tentative cpPKs and 21 tentative cpPPs. However, test sets of 9 tentative cpPKs and 13 tentative cpPPs contain only 2 and 7 genuine cpPKs and cpPPs, respectively, based on experimental subcellular localization of their N-termini fused to the reporter protein RFP. Taken together, the set of enzymes known to be involved in the reversible phosphorylation of chloroplast proteins in A. thaliana comprises altogether now 6 cpPKs and 9 cpPPs, the function of which needs to be determined in future by functional genomics approaches. This includes the calcium-regulated PK CIPK13 which we found to be located in the chloroplast, indicating that calcium-dependent signal transduction pathways also operate in this organelle.

AB - Protein phosphorylation is a major mode of regulation of metabolism, gene expression and cell architecture. In chloroplasts, reversible phosphorylation of proteins is known to regulate a number of prominent processes, for instance photosynthesis, gene expression and starch metabolism. The complements of the involved chloroplast protein kinases (cpPKs) and phosphatases (cpPPs) are largely unknown, except 6 proteins (4 cpPKs and 2 cpPPs) which have been experimentally identified so far. We employed combinations of programs predicting N-terminal chloroplast transit peptides (cTPs) to identify 45 tentative cpPKs and 21 tentative cpPPs. However, test sets of 9 tentative cpPKs and 13 tentative cpPPs contain only 2 and 7 genuine cpPKs and cpPPs, respectively, based on experimental subcellular localization of their N-termini fused to the reporter protein RFP. Taken together, the set of enzymes known to be involved in the reversible phosphorylation of chloroplast proteins in A. thaliana comprises altogether now 6 cpPKs and 9 cpPPs, the function of which needs to be determined in future by functional genomics approaches. This includes the calcium-regulated PK CIPK13 which we found to be located in the chloroplast, indicating that calcium-dependent signal transduction pathways also operate in this organelle.

KW - Journal Article

U2 - 10.2174/138920208784340740

DO - 10.2174/138920208784340740

M3 - Journal article

C2 - 19440515

VL - 9

SP - 184

EP - 190

JO - Current Genomics

JF - Current Genomics

SN - 1389-2029

IS - 3

ER -

ID: 174440557