Tags

Type your tag names separated by a space and hit enter

Mutational analysis of the input domain of the VirA protein of Agrobacterium tumefaciens.
J Bacteriol. 1996 Feb; 178(4):961-70.JB

Abstract

The transmembrane sensor protein VirA activates VirG in response to high levels of acetosyringone (AS). In order to respond to low levels of AS, VirA requires the periplasmic sugar-binding protein ChvE and monosaccharides released from plant wound sites. To better understand how VirA senses these inducers, the C58 virA gene was randomly mutagenized, and 14 mutants defective in vir gene induction and containing mutations which mapped to the input domain of VirA were isolated. Six mutants had single missense mutatiions in three widely separated areas of the periplasmic domain. Eight mutants had mutations in or near an amphipathic helix, TM1, or TM2. Four of the mutations in the periplasmic domain, when introduced into the corresponding A6 virA sequence, caused a specific defect in the vir gene response to glucose. This suggests that most of the periplasmic domain is required for the interaction with, or response to, ChvE. Three of the mutations from outside the periplasmic domain, one from each transmembrane domain and one from the amphiphathic helix, were made in A6 virA. These mutants were defective in the vir gene response to AS. These mutations did not affect the stability or topology of VirA or prevent dimerization; therefore, they may interfere with detection of AS or transmission of the signals to the kinase domain. Characterization of C58 chvE mutants revealed that, unlike A6 VirA, C58 VirA requires ChvE for activation of the vir genes.

Authors+Show Affiliations

Department of Microbiology, University of Washington, Seattle 98195, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

8576069

Citation

Doty, S L., et al. "Mutational Analysis of the Input Domain of the VirA Protein of Agrobacterium Tumefaciens." Journal of Bacteriology, vol. 178, no. 4, 1996, pp. 961-70.
Doty SL, Yu MC, Lundin JI, et al. Mutational analysis of the input domain of the VirA protein of Agrobacterium tumefaciens. J Bacteriol. 1996;178(4):961-70.
Doty, S. L., Yu, M. C., Lundin, J. I., Heath, J. D., & Nester, E. W. (1996). Mutational analysis of the input domain of the VirA protein of Agrobacterium tumefaciens. Journal of Bacteriology, 178(4), 961-70.
Doty SL, et al. Mutational Analysis of the Input Domain of the VirA Protein of Agrobacterium Tumefaciens. J Bacteriol. 1996;178(4):961-70. PubMed PMID: 8576069.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mutational analysis of the input domain of the VirA protein of Agrobacterium tumefaciens. AU - Doty,S L, AU - Yu,M C, AU - Lundin,J I, AU - Heath,J D, AU - Nester,E W, PY - 1996/2/1/pubmed PY - 1996/2/1/medline PY - 1996/2/1/entrez SP - 961 EP - 70 JF - Journal of bacteriology JO - J. Bacteriol. VL - 178 IS - 4 N2 - The transmembrane sensor protein VirA activates VirG in response to high levels of acetosyringone (AS). In order to respond to low levels of AS, VirA requires the periplasmic sugar-binding protein ChvE and monosaccharides released from plant wound sites. To better understand how VirA senses these inducers, the C58 virA gene was randomly mutagenized, and 14 mutants defective in vir gene induction and containing mutations which mapped to the input domain of VirA were isolated. Six mutants had single missense mutatiions in three widely separated areas of the periplasmic domain. Eight mutants had mutations in or near an amphipathic helix, TM1, or TM2. Four of the mutations in the periplasmic domain, when introduced into the corresponding A6 virA sequence, caused a specific defect in the vir gene response to glucose. This suggests that most of the periplasmic domain is required for the interaction with, or response to, ChvE. Three of the mutations from outside the periplasmic domain, one from each transmembrane domain and one from the amphiphathic helix, were made in A6 virA. These mutants were defective in the vir gene response to AS. These mutations did not affect the stability or topology of VirA or prevent dimerization; therefore, they may interfere with detection of AS or transmission of the signals to the kinase domain. Characterization of C58 chvE mutants revealed that, unlike A6 VirA, C58 VirA requires ChvE for activation of the vir genes. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/8576069/Mutational_analysis_of_the_input_domain_of_the_VirA_protein_of_Agrobacterium_tumefaciens_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=8576069 DB - PRIME DP - Unbound Medicine ER -