Comparative study of the life cycle dependent post-translation modifications of protein synthesis elongation factor Tu present in the membrane proteome of streptomycetes and mycobacteria
Language English Country United States Media print-electronic
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Cell Membrane chemistry enzymology metabolism MeSH
- Peptide Elongation Factor Tu isolation & purification metabolism MeSH
- Phosphorylation MeSH
- Mycobacterium smegmatis chemistry enzymology metabolism MeSH
- Protein Processing, Post-Translational * MeSH
- Protein Kinases isolation & purification metabolism MeSH
- Streptomyces chemistry enzymology metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Peptide Elongation Factor Tu MeSH
- Protein Kinases MeSH
We present the results of analysis of membrane phosphoproteomes from individual morphological stages of Streptomyces coelicolor that reflect developmentally dependent heterogeneity and phosphorylation of intrinsic and externally added purified Strepomyces aureofaciens EF-Tu. Fast growing nonpathogenic Mycobacterium smegmatis was used as a non-differentiating actinomycetes comparative model. Streptomycetes membrane fraction was found to contain protein kinase(s) catalyzing phosphorylation of both its own and an externally added EF-Tu, whereas Mycobacterium membrane fraction contains protein kinase phosphorylating only its own EF-Tu.
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