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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.


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