Evidence of tyrosine kinase activity in the photosynthetic bacterium Rhodospirillum rubrum
| Autor: | Loreto Holuigue, Héctor A. Lucero, Mónica Torruella, Rubén H. Vallejos |
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| Rok vydání: | 1985 |
| Předmět: |
Chemical Phenomena
Biophysics Alkalies Biology Rhodospirillum rubrum Biochemistry Substrate Specificity chemistry.chemical_compound Protein phosphorylation Amino Acids Phosphorylation Tyrosine Sodium dodecyl sulfate Protein kinase A Molecular Biology Polyacrylamide gel electrophoresis Cell Biology Protein-Tyrosine Kinases Phosphoproteins biology.organism_classification Chemistry chemistry Autoradiography Electrophoresis Polyacrylamide Gel Protein Kinases Tyrosine kinase |
| Zdroj: | Biochemical and Biophysical Research Communications. 126:685-691 |
| ISSN: | 0006-291X |
| Popis: | The photosynthetic bacterium Rohodospirillum rubrum evidence tyrosine protein phosphorylation under photoautotrophic conditions in the presence of { 32 P}Pi. The stability to alkaline treatment of the { 32 P} bound to the cell-free extract proteins suggested that tyrosine residues were carrying the labelling. One- and two-dimensional high voltage paper electrophoresis analysis revealed that such extracts do contain { 32 P}-phosphotyrosine residues. Furthermore, the association of alkali stable { 32 P} bound to specific proteins of the cell-free extract was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis combined with KOH treatment of the gel. A definite argument in favor of protein kinase(s) phosphorylating tyrosine residues in R.rubrum proteins was obtained by partial purification of a tyrosine kinase activity from cell-free extract capable of phosphorylating synthetic peptides that only contain a single tyrosine residue as phosphate acceptor. |
| Databáze: | OpenAIRE |
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