MRY, A TRANS-ACTING POSITIVE REGULATOR OF THE M-PROTEIN GENE OF STREPTOCOCCUS-PYOGENES WITH SIMILARITY TO THE RECEPTOR PROTEINS OF 2-COMPONENT REGULATORY SYSTEMS
MRY, A TRANS-ACTING POSITIVE REGULATOR OF THE M-PROTEIN GENE OF STREPTOCOCCUS-PYOGENES WITH SIMILARITY TO THE RECEPTOR PROTEINS OF 2-COMPONENT REGULATORY SYSTEMS
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DOI:
10.1128/jb.173.8.2617-2624.1991
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发表时间:
1991-04-01
影响因子:
3.2
通讯作者:
SCOTT, JR
中科院分区:
文献类型:
--
作者:
PEREZCASAL, J;CAPARON, MG;SCOTT, JR
In the Streptococcus pyogenes M6 strain D471, an insertion of the conjugative transposon Tn916 into a region 2 kb upstream of the promoter of emm6 (the structural gene for the M protein) rendered the strain M negative (M. G. Caparon and J. R. Scott, Proc. Natl. Acad. Sci. USA 84:8677-8681, 1987). In the present work, we show that this insertion mutation, mry-1, is 244 bp upstream of an open reading frame encoding a protein we call Mry. This protein is visible on a gel after transcription and translation in vitro. We have developed a technique for complementation analysis in S. pyogenes and have used it to show that the wild-type mry gene is dominant to two mutant alleles. This dominance indicates that Mry acts in trans as a positive regulator of the emm6 gene. The translated DNA sequence of mry has two regions of similarity to the motif common to the receptor protein of two-component regulatory systems. In addition, the N terminus of Mry has two regions resembling a helix-turn-helix motif. Mry does not appear to be a global regulator of virulence determinants in the group A streptococcus because there is no effect of the mry-1 mutation on production of the hyaluronic acid capsule or streptokinase.