Skip Navigation

This Article
Right arrow Print PDF (1097K)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (49)
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Koronakis, V.
Right arrow Articles by Hughes, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Koronakis, V.
Right arrow Articles by Hughes, C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1988, Vol. 16, No. 11 4789-4800
© 1988

Articles

Expression of the E.coli hemolysin secretion gene hlyB involves transcript anti-termination within the hly operon

Vassilis Koronakis, Michael Cross and Colin Hughes

Department of Pathology, Cambridge University Tennis Court Road, Cambridge, CB2 1QP, UK

Received April 7, 1988. Revised May 12, 1988. Accepted May 12, 1988.

The genes hly A and hly B dictating synthesis and secretion of hemolytic toxin by Escherichia coli are transcribed as part of an operon hly C,hly A,hly B but are separated by an inverted repeat and poly-T sequence characteristic of a rho-independent terminator. The hly A-hly B intergenic sequence caused a reduction of in vivo transcriptional read-through from the gal promoter into gal K when inserted in the pKG1900 terminator-probe vector and also in vitro 3' to the bacteriophage T7 ø10 promotor. Hybridisation of mRNA generated by the hly determinant of recombinant DNA pBR202–312 to an antisense RNA probe spanning the hly intergenic sequence revealed specific termination of 80% of in vivo hly transcripts within the poly-T sequence, immediately preceeding the hly B translation start. Extension of the hly determinant with 3.5kbp of hly promoter-proximal DNA sequence raised intracellular and cell-free hemolytic activity 3-fold and 20-fold respectively and increased markedly the secretion of the 107Kd hemolysin protein (HlyA). Parallel hybridisation of in vivo mRNA to hly A and hly B antisense probes revealed that levels ofhlyA and hlyB mRNA were Increased by approximately 3-fold and 90-fold. The dramatically enhanced level of hly B mRNA resulted primarily from specific suppression of transcription termination at the intergenic rho-independent terminator from 80% to 1%, thus allowing virtually all hly A transcripts to elongate into hly B.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Nucleic Acids ResHome page
V. Svetlov, G. A. Belogurov, E. Shabrova, D. G. Vassylyev, and I. Artsimovitch
Allosteric control of the RNA polymerase by the elongation factor RfaH
Nucleic Acids Res., September 27, 2007; 35(17): 5694 - 5705.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
A. L. Pimenta, K. Racher, L. Jamieson, M. A. Blight, and I. B. Holland
Mutations in HlyD, Part of the Type 1 Translocator for Hemolysin Secretion, Affect the Folding of the Secreted Toxin
J. Bacteriol., November 1, 2005; 187(21): 7471 - 7480.
[Abstract] [Full Text] [PDF]

Home page
 J. Bacteriol.Home page
H. D. Carter, V. Svetlov, and I. Artsimovitch
Highly Divergent RfaH Orthologs from Pathogenic Proteobacteria Can Substitute for Escherichia coli RfaH both In Vivo and In Vitro
J. Bacteriol., May 1, 2004; 186(9): 2829 - 2840.
[Abstract] [Full Text] [PDF]

Home page
 ScienceHome page
P Stanley, L. Packman, V Koronakis, and C Hughes
Fatty acylation of two internal lysine residues required for the toxic activity of Escherichia coli hemolysin
Science, December 23, 1994; 266(5193): 1992 - 1996.
[Abstract] [PDF]

Home page
 J. Biol. Chem.Home page
C. Guzman-Verri, E. Chaves-Olarte, F. Garcia, S. Arvidson, and E. Moreno
In Vivo Proteolytic Degradation of the Escherichia coli Acyltransferase HlyC
J. Biol. Chem., May 11, 2001; 276(20): 16660 - 16666.
[Abstract] [Full Text] [PDF]


Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.