ArticleJournal of bacteriology1992
Tyrosine phosphorylation of a membrane protein from Pseudomonas solanacearum.
Article in Journal of bacteriology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 28 citations in OpenAlex.
- Protein tyrosine kinases in bacterial pathogens are associated with virulence and production of exopolysaccharide.The EMBO journal · 1999Article
- Tyrosine phosphorylation is required for ehrlichial internalization and replication in P388D1 cells.Infection and immunity · 1997Article
- Fancy meeting you here! A fresh look at "prokaryotic" protein phosphorylation.Journal of bacteriology · 1996Review
- Tyrosine phosphorylation in Myxococcus xanthus, a multicellular prokaryote.Journal of bacteriology · 1996Article
- Isolation and cloning of a protein-serine/threonine phosphatase from an archaeon.Journal of bacteriology · 1995Article
- Tyrosine phosphate in a- and b-type flagellins of Pseudomonas aeruginosa.Journal of bacteriology · 1993Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have investigated a tyrosine kinase activity from Pseudomonas solanacearum, an economically important plant pathogen. In vitro incubation of membrane fractions with [gamma-32P]ATP and subsequent sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed an 85-kDa phosphoprotein. Phosphorylation of this protein on tyrosine residues was demonstrated by phosphoamino acid analysis of base hydrolysis products and by immunoanalysis of Western blots (immunoblots) with antiphosphotyrosine monoclonal antibody. In vitro incubation of membranes with ATP was not required for recognition by the antibody, indicating that the 85-kDa protein is phosphorylated in vivo. These results demonstrate that membranes from P. solanacearum exhibit a tyrosine kinase activity toward an endogenous membrane protein. This bacterium provides an opportunity to study the structure and function of a prokaryotic tyrosine kinase.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.