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PMID: 8366057 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The chimeric VirA-tar receptor protein is locked into a highly responsive state.

Journal of bacteriology ·Vol. 175 ·No. 17 ·1993-09-00 ·Pages 5706-9

Turk SC, van Lange RP, Sonneveld E, Hooykaas PJ

Abstract

The wild-type VirA protein is known to be responsive not only to phenolic compounds but also to sugars via the ChvE protein (G. A. Cangelosi, R. G. Ankenbauer, and E. W. Nester, Proc. Natl. Acad. Sci. USA 87:6708-6712, 1990, and N. Shimoda, A. Toyoda-Yamamoto, J. Nagamine, S. Usami, M. Katayama, Y. Sakagami, and Y. Machida, Proc. Natl. Acad. Sci. USA 87:6684-6688, 1990). It is shown here that the mutant VirA(Ser-44, Arg-45) protein and the chimeric VirA-Tar protein are no longer responsive to sugars and the ChvE protein. However, whereas the chimeric VirA-Tar protein was found to be locked in a highly responsive state, the VirA(Ser-44, Arg-45) mutant protein appeared to be locked in a low responsive state. This difference turned out to be important for tumorigenicity of the host strains in virulence assays on Kalanchoë daigremontiana.

MeSH Terms
Agrobacterium tumefaciens/genetics,metabolism Bacterial Proteins/genetics,metabolism Chemoreceptor Cells Cloning, Molecular Escherichia coli Proteins Membrane Proteins/genetics,metabolism Phenotype Plants/microbiology Receptors, Cell Surface Recombinant Fusion Proteins/genetics,metabolism Restriction Mapping Virulence Factors
Chemicals
Bacterial Proteins Escherichia coli Proteins Membrane Proteins Receptors, Cell Surface Recombinant Fusion Proteins Tar protein, E coli Virulence Factors
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Turk S C
Clusius Laboratory, Leiden University, The Netherlands.
van Lange R P
Sonneveld E
Hooykaas P J
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24 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.175.17.5706-5709.1993
Published
1993-09-00
Pages
5706-9
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC206631
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.175.17.5706-5709.1993 PMC Full Text View journal details
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