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Comparison of the leader sequences of four group A streptococcal M protein genes
Author(s) -
E Haanes-Fritz,
Werner Kraus,
Vickers Burdett,
James B. Dale,
E H Beachey,
P. Patrick Cleary
Publication year - 1988
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/16.10.4667
Subject(s) - biology , gene , genetics , signal peptide , peptide sequence , amino acid , dna , nucleic acid sequence , sequence alignment , sequence (biology) , conserved sequence , microbiology and biotechnology
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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