| pubmed-article:19440515 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19440515 | lifeskim:mentions | umls-concept:C0162740 | lld:lifeskim |
| pubmed-article:19440515 | lifeskim:mentions | umls-concept:C0008266 | lld:lifeskim |
| pubmed-article:19440515 | lifeskim:mentions | umls-concept:C0031678 | lld:lifeskim |
| pubmed-article:19440515 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
| pubmed-article:19440515 | lifeskim:mentions | umls-concept:C0038951 | lld:lifeskim |
| pubmed-article:19440515 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:19440515 | pubmed:dateCreated | 2009-5-14 | lld:pubmed |
| pubmed-article:19440515 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:19440515 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19440515 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19440515 | pubmed:status | PubMed-not-MEDLINE | lld:pubmed |
| pubmed-article:19440515 | pubmed:month | May | lld:pubmed |
| pubmed-article:19440515 | pubmed:issn | 1389-2029 | lld:pubmed |
| pubmed-article:19440515 | pubmed:author | pubmed-author:PribilMM | lld:pubmed |
| pubmed-article:19440515 | pubmed:author | pubmed-author:DietzmannAA | lld:pubmed |
| pubmed-article:19440515 | pubmed:author | pubmed-author:LeisterDD | lld:pubmed |
| pubmed-article:19440515 | pubmed:author | pubmed-author:ZühlkeJJ | lld:pubmed |
| pubmed-article:19440515 | pubmed:author | pubmed-author:SchliebnerII | lld:pubmed |
| pubmed-article:19440515 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:19440515 | pubmed:volume | 9 | lld:pubmed |
| pubmed-article:19440515 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19440515 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19440515 | pubmed:pagination | 184-90 | lld:pubmed |
| pubmed-article:19440515 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:19440515 | pubmed:articleTitle | A Survey of Chloroplast Protein Kinases and Phosphatases in Arabidopsis thaliana. | lld:pubmed |
| pubmed-article:19440515 | pubmed:affiliation | Lehrstuhl für Botanik, Department Biologie, Ludwig-Maximilians-Universität München, Menzinger Str. 67, 80638 München, Germany. | lld:pubmed |
| pubmed-article:19440515 | pubmed:publicationType | Journal Article | lld:pubmed |
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