JBC Advanced Peptides, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M110178200 on March 6, 2002

J. Biol. Chem., Vol. 277, Issue 20, 17630-17637, May 17, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/20/17630    most recent
M110178200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Stapleton, M. R.
Right arrow Articles by Green, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stapleton, M. R.
Right arrow Articles by Green, J.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Interaction of the Salmonella typhimurium Transcription and Virulence Factor SlyA with Target DNA and Identification of Members of the SlyA Regulon*

Melanie R. StapletonDagger , Valia A. NorteDagger , Robert C. Read§, and Jeffrey GreenDagger

From Dagger  the Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, United Kingdom and the § Division of Genomic Medicine, University of Sheffield Medical School, Sheffield S10 2RX United Kingdom

The SlyA protein from Salmonella typhimurium is a transcription factor that contributes to virulence. It is shown that a slyA mutant is attenuated in the presence of murine macrophages compared with the parent strain. Moreover, after growth in minimal medium, survival of the slyA mutant was reduced. Altered levels of flagellin (fliC), PagC, IroN, and outer membrane proteins suggest that the slyA mutation affects the surface properties of Salmonella. The isolated SlyA protein is a cofactor-free homodimer that recognizes five sites within the promoter region of the slyA gene. One of these sites contained a near perfect inverted repeat TTAGCAAGCTAA. The other four sites contained related sequences. Occupation of the SlyA sites in the slyA promoter prevented open-complex formation, consistent with the pattern of slyA::lacZ expression parental and slyA mutant strains. By combining the footprinting data with potential SlyA binding sites recovered from a pool of random DNA sequences, a consensus was defined and used to probe the NIH Salmonella unfinished genomes data base. These searches revealed the presence of consensus SlyA sites upstream of omp, ispA, xseB, slyA, and a gene encoding a protein with homology to a hemagglutinin. Accordingly, transcription of an omp::lacZ fusion was reduced in a slyA mutant. Given the difficulties in obtaining a comprehensive picture of intracellular gene expression, the definition of the DNA sequence recognized by a transcription factor (SlyA) that is essential for survival in the macrophage environment should allow a complete regulon of genes with altered expression upon exposure to macrophages to be determined once the S. typhimurium genome annotation is complete.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed. Tel.: 44-114-2224403; Fax: 44-114-2728697; E-mail: jeff.green@sheffield.ac.uk.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
H. Song, W. Kong, N. Weatherspoon, G. Qin, W. Tyler, J. Turk, R. Curtiss III, and Y. Shi
Modulation of the Regulatory Activity of Bacterial Two-component Systems by SlyA
J. Biol. Chem., October 17, 2008; 283(42): 28158 - 28168.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
A. A. Larrea, I. M. Pedroso, A. Malhotra, and R. S. Myers
Identification of two conserved aspartic acid residues required for DNA digestion by a novel thermophilic Exonuclease VII in Thermotoga maritima
Nucleic Acids Res., October 1, 2008; 36(18): 5992 - 6003.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
D. M. Stoebel, A. Free, and C. J. Dorman
Anti-silencing: overcoming H-NS-mediated repression of transcription in Gram-negative enteric bacteria
Microbiology, September 1, 2008; 154(9): 2533 - 2545.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. C. Perez, T. Latifi, and E. A. Groisman
Overcoming H-NS-mediated Transcriptional Silencing of Horizontally Acquired Genes by the PhoP and SlyA Proteins in Salmonella enterica
J. Biol. Chem., April 18, 2008; 283(16): 10773 - 10783.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
D. Corbett, H. J. Bennett, H. Askar, J. Green, and I. S. Roberts
SlyA and H-NS Regulate Transcription of the Escherichia coli K5 Capsule Gene Cluster, and Expression of slyA in Escherichia coli Is Temperature-dependent, Positively Autoregulated, and Independent of H-NS
J. Biol. Chem., November 16, 2007; 282(46): 33326 - 33335.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
W. W. Navarre, M. McClelland, S. J. Libby, and F. C. Fang
Silencing of xenogeneic DNA by H-NS--facilitation of lateral gene transfer in bacteria by a defense system that recognizes foreign DNA
Genes & Dev., June 15, 2007; 21(12): 1456 - 1471.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
K. Wei, D.-J. Tang, Y.-Q. He, J.-X. Feng, B.-L. Jiang, G.-T. Lu, B. Chen, and J.-L. Tang
hpaR, a Putative marR Family Transcriptional Regulator, Is Positively Controlled by HrpG and HrpX and Involved in the Pathogenesis, Hypersensitive Response, and Extracellular Protease Production of Xanthomonas campestris Pathovar campestris
J. Bacteriol., March 1, 2007; 189(5): 2055 - 2062.
[Abstract] [Full Text] [PDF]


Home page
MicrobiologyHome page
N. Okada, Y. Oi, M. Takeda-Shitaka, K. Kanou, H. Umeyama, T. Haneda, T. Miki, S. Hosoya, and H. Danbara
Identification of amino acid residues of Salmonella SlyA that are critical for transcriptional regulation
Microbiology, February 1, 2007; 153(2): 548 - 560.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
C. von Rhein, K.-P. Hunfeld, and A. Ludwig
Serologic Evidence for Effective Production of Cytolysin A in Salmonella enterica Serovars Typhi and Paratyphi A during Human Infection
Infect. Immun., November 1, 2006; 74(11): 6505 - 6508.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. M. Reynolds, A. A. Ribeiro, S. C. McGrath, R. J. Cotter, C. R. H. Raetz, and M. S. Trent
An Outer Membrane Enzyme Encoded by Salmonella typhimurium lpxR That Removes the 3'-Acyloxyacyl Moiety of Lipid A
J. Biol. Chem., August 4, 2006; 281(31): 21974 - 21987.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
S. A. Linehan, A. Rytkonen, X.-J. Yu, M. Liu, and D. W. Holden
SlyA Regulates Function of Salmonella Pathogenicity Island 2 (SPI-2) and Expression of SPI-2-Associated Genes
Infect. Immun., July 1, 2005; 73(7): 4354 - 4362.
[Abstract] [Full Text] [PDF]


Home page
Infect. Immun.Home page
M.-J. Ferrandiz, K. Bishop, P. Williams, and H. Withers
HosA, a Member of the SlyA Family, Regulates Motility in Enteropathogenic Escherichia coli
Infect. Immun., March 1, 2005; 73(3): 1684 - 1694.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Shi, T. Latifi, M. J. Cromie, and E. A. Groisman
Transcriptional Control of the Antimicrobial Peptide Resistance ugtL Gene by the Salmonella PhoP and SlyA Regulatory Proteins
J. Biol. Chem., September 10, 2004; 279(37): 38618 - 38625.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
C. Rouanet, S. Reverchon, D. A. Rodionov, and W. Nasser
Definition of a Consensus DNA-binding Site for PecS, a Global Regulator of Virulence Gene Expression in Erwinia chrysanthemi and Identification of New Members of the PecS Regulon
J. Biol. Chem., July 16, 2004; 279(29): 30158 - 30167.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
N. R. Wyborn, M. R. Stapleton, V. A. Norte, R. E. Roberts, J. Grafton, and J. Green
Regulation of Escherichia coli Hemolysin E Expression by H-NS and Salmonella SlyA
J. Bacteriol., March 15, 2004; 186(6): 1620 - 1628.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
V. A. Norte, M. R. Stapleton, and J. Green
PhoP-Responsive Expression of the Salmonella enterica Serovar Typhimurium slyA Gene
J. Bacteriol., June 15, 2003; 185(12): 3508 - 3514.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.