JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Choi, S H
Right arrow Articles by Greenberg, E P
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Choi, S H
Right arrow Articles by Greenberg, E P
J Bacteriol. 1992 June; 174(12): 4064-4069

research-article

Genetic dissection of DNA binding and luminescence gene activation by the Vibrio fischeri LuxR protein.

S H Choi and E P Greenberg

Department of Microbiology, University of Iowa, Iowa City 52242.

ABSTRACT

The Vibrio fischeri luminescence (lux) genes are regulated by the 250-amino-acid-residue LuxR protein and a V. fischeri metabolite termed autoinducer. The V. fischeri lux regulon consists of two divergently transcribed units. Autoinducer and LuxR activate transcription of the luxICDABE operon and autoregulate the luxR transcriptional unit. LuxR proteins with C-terminal truncations of up to 40 amino acid residues coded by plasmids with luxR 3'-deletion mutations are functional in negative autoregulation as demonstrated by using a luxR::lacZ transcriptional fusion as a luxR promoter probe in Escherichia coli. The truncated LuxR proteins showed little or no ability to activate transcription of luxICDABE, as indicated by using luminescence as a sensitive indicator of promoter strength in E. coli. Besides having no detectable activity as positive regulators of luxICDABE, LuxR proteins with C-terminal truncations of more than 40 amino acid residues had reduced or no detectable activity as negative autoregulators. The results suggest that amino acid residues in LuxR prior to no. 211 are sufficient for lux DNA binding. Residues in the region of 211 to 250 constitute a C-terminal tail that appears to be involved in activation of luxICDABE transcription either by interacting physically with the transcription initiation complex or by affecting lux DNA in the vicinity of the promoter.

J Bacteriol. 1992 June; 174(12): 4064-4069




This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1992 by the American Society for Microbiology. All rights reserved.