A phyloproteomic characterization ofin vitro autophosphorylation in calcium-dependent protein kinases
説明
Calcium-dependent protein kinases (CDPKs) are a novel class of signaling molecules that have been broadly implicated in relaying specific calcium-mediated responses to biotic and abiotic stress as well as developmental cues in both plants and protists. Calcium-dependent autophosphorylation has been observed in almost all CDPKs examined, but a physiological role for autophosphorylation has not been demonstrated. To date, only a handful of autophosphorylation sites have been mapped to specific residues within CDPK amino acid sequences. In an attempt to gain further insight into this phenomenon, we have mapped autophosphorylation sites and compared these phosphorylation patterns among multiple CDPK isoforms. From eight CDPKs and two CDPK-related kinases from Arabidopsis thaliana and Plasmodium falciparum, 31 new autophosphorylation sites were characterized, which in addition to the previously described sites, allowed the identification of five conserved loci. Of the 35 total sites analyzed approximately one-half were observed in the N-terminal variable domain. Homology models were generated for the protein kinase and calmodulin-like domains, each containing two of the five conserved sites, to allow intelligent speculation regarding subsequent lines of investigation.
収録刊行物
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- PROTEOMICS
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PROTEOMICS 6 (12), 3649-3664, 2006-06
Wiley
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キーワード
- Models, Molecular
- Proteome
- Amino Acid Motifs
- Molecular Sequence Data
- Plasmodium falciparum
- Arabidopsis
- In Vitro Techniques
- Escherichia coli
- Animals
- Amino Acid Sequence
- Amino Acids
- Phosphorylation
- Conserved Sequence
- Plant Proteins
- Sequence Homology, Amino Acid
- Hydrolysis
- Plants
- Protein Structure, Tertiary
- Isoenzymes
- Data Interpretation, Statistical
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
- Calcium
- Protein Kinases
詳細情報 詳細情報について
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- CRID
- 1363107368447157632
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- ISSN
- 16159861
- 16159853
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- PubMed
- 16758442
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- データソース種別
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- Crossref
- OpenAIRE