Tyrosine phosphorylation in Escherichia coli
Tyrosine phosphorylation in Escherichia coli
The phosphorylation on tyrosine of a protein in Escherichia coli both in vivo and in vitro was revealed by recognition by anti-phosphotyrosine antibodies, labelling with [gamma-32P]ATP, and phosphoamino acid analysis. This protein, which we name TypA, is the product of the o591 reading frame as revealed by N-terminal sequencing and antibody cross-reactivity. Inactivation of typA altered the patterns of protein synthesis during both exponential growth and carbon starvation. These alterations included the disappearance of an acidic isoform of both the universal stress protein UspA and carbon starvation protein Csp15, and increased synthesis of the histone-like protein H-NS. The sequence of TypA from strain K-12 differs from that of an enteropathogenic strain in six amino acid residues and the protein is three residues shorter. We propose that TypA interacts with global regulatory networks and that its phosphorylation may be relevant to pathogenesis.
Adenosine Triphosphate/metabolism, Bacterial Proteins/genetics, Escherichia coli/genetics, Escherichia coli Proteins, GTP Phosphohydrolases, Heat-Shock Proteins/immunology, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Radioactive Tracers, Tyrosine/immunology
1045-51
Freestone, P
1227295c-64f7-4a11-bc5d-045bcd35e96f
Trinei, M
a92c8f76-50c4-4271-ad2d-566713a54c5d
Clarke, S C
f7d7f7a2-4b1f-4b36-883a-0f967e73fb17
Nyström, T
d21c9d76-6681-408c-8b6e-0c76b7ff6eb9
Norris, V
1e6846fe-9418-4f08-8f79-7aa1d57f826d
26 June 1998
Freestone, P
1227295c-64f7-4a11-bc5d-045bcd35e96f
Trinei, M
a92c8f76-50c4-4271-ad2d-566713a54c5d
Clarke, S C
f7d7f7a2-4b1f-4b36-883a-0f967e73fb17
Nyström, T
d21c9d76-6681-408c-8b6e-0c76b7ff6eb9
Norris, V
1e6846fe-9418-4f08-8f79-7aa1d57f826d
Freestone, P, Trinei, M, Clarke, S C, Nyström, T and Norris, V
(1998)
Tyrosine phosphorylation in Escherichia coli.
Journal of Molecular Biology, 279 (5), .
(doi:10.1006/jmbi.1998.1836).
Abstract
The phosphorylation on tyrosine of a protein in Escherichia coli both in vivo and in vitro was revealed by recognition by anti-phosphotyrosine antibodies, labelling with [gamma-32P]ATP, and phosphoamino acid analysis. This protein, which we name TypA, is the product of the o591 reading frame as revealed by N-terminal sequencing and antibody cross-reactivity. Inactivation of typA altered the patterns of protein synthesis during both exponential growth and carbon starvation. These alterations included the disappearance of an acidic isoform of both the universal stress protein UspA and carbon starvation protein Csp15, and increased synthesis of the histone-like protein H-NS. The sequence of TypA from strain K-12 differs from that of an enteropathogenic strain in six amino acid residues and the protein is three residues shorter. We propose that TypA interacts with global regulatory networks and that its phosphorylation may be relevant to pathogenesis.
This record has no associated files available for download.
More information
Published date: 26 June 1998
Keywords:
Adenosine Triphosphate/metabolism, Bacterial Proteins/genetics, Escherichia coli/genetics, Escherichia coli Proteins, GTP Phosphohydrolases, Heat-Shock Proteins/immunology, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Radioactive Tracers, Tyrosine/immunology
Identifiers
Local EPrints ID: 453821
URI: http://eprints.soton.ac.uk/id/eprint/453821
ISSN: 0022-2836
PURE UUID: 0259cfe8-0c48-467f-8c5e-16323f47d919
Catalogue record
Date deposited: 24 Jan 2022 17:55
Last modified: 17 Mar 2024 03:07
Export record
Altmetrics
Contributors
Author:
P Freestone
Author:
M Trinei
Author:
T Nyström
Author:
V Norris
Download statistics
Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.
View more statistics
