Skip Navigation

This Article
Right arrow Print PDF (569K)
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 (40)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Haanes-Fritz, E.
Right arrow Articles by Cleary, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Haanes-Fritz, E.
Right arrow Articles by Cleary, P.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1988, Vol. 16, No. 10 4667-4677
© 1988

Articles

Comparison of the leader sequences of four group A streptococcal M protein genes

Elizabeth Haanes-Fritz*, Werner Kraus1, Vickers Burdett2, James B. Dale1, Edwin H. Beachey1 and Patrick Cleary

Department of Microbiology, University of Minnesota Minneapolis, MN 55455 1Veterans Administration Medical Center and University of Tennessee Memphis, TN 38104 2Department of Microbiology, Duke University Medical Center Durham, NC 27710, USA

*To whom correspondence should be addressed

Received December 23, 1988. Revised April 14, 1988. Accepted April 14, 1988.

The 5' portions and flanking sequences of genes encoding types 1, 12, 24, and 6 M proteins were compared. Although the DNA sequences encoding the amino-termini of the mature M proteins had no obvious similarity, upstream sequences, and those encoding the signal peptides (leader sequences) of the four M protein genes had considerable similarity. In general, the 5' ends of all the leader sequences were more conserved than the 3' ends, although the M6 and M24 leader sequences had identical 3'ends. Sequence similarity among the deduced amino acid sequences of the four signal peptides was more extensive than the corresponding DNA sequences. We found that strict DNA similarity among all four sequences extended only to the ends of the hydrophilic amino-terminal regions of the signal peptides, but that amino acid sequence conservation continued to the ends of the respective hydrophobic cores. With the exception of the M6 and M24 sequences, the regions adjacent to the signal peptidase cleavage sites were highly variable.


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
 Infect. Immun.Home page
C.-H. Wang, C.-Y. Lin, Y.-H. Luo, P.-J. Tsai, Y.-S. Lin, M. T. Lin, W.-J. Chuang, C.-C. Liu, and J.-J. Wu
Effects of Oligopeptide Permease in Group A Streptococcal Infection
Infect. Immun., May 1, 2005; 73(5): 2881 - 2890.
[Abstract] [Full Text] [PDF]

Home page
 Microbiol. Mol. Biol. Rev.Home page
W. W. Navarre and O. Schneewind
Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope
Microbiol. Mol. Biol. Rev., March 1, 1999; 63(1): 174 - 229.
[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.