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J Biol Chem, Vol. 274, Issue 8, 4786-4793, February 19, 1999
From the Department of Microbiology and Immunology, Wake Forest
University School of Medicine,
Winston-Salem, North Carolina 27157
Hyaluronic acid production by group A
streptococci is regulated by transcriptional control. In this study,
transposon mutagenesis of an unencapsulated strain yielded an
encapsulated mutant. Two genes homologous to sensors and response
regulators of bacterial two-component systems were identified
downstream of the transposon insertion. Inactivation of the putative
sensor gene, csrS, in three different unencapsulated
strains yielded encapsulated mutant strains. Electrophoretic mobility
shift assays determined factor(s) in a cytoplasmic extract of an
unencapsulated group A streptococcal strain was binding to a
double-stranded DNA fragment derived from the has operon
promoter. In contrast, similarly prepared cytoplasmic extracts from a
csrS deletion mutant did not shift the fragment. The
putative response regulator, CsrR, was partially purified and was shown
to bind the has operon promoter fragment. The affinity and
specificity of CsrR for the fragment were increased significantly after
incubation with acetyl phosphate. DNase I footprinting determined that
the acetyl phosphate-treated CsrR was binding to key sequences in the
promoter and the coding region of hasA. Therefore, a
two-component system is repressing the production of hyaluronic acid in
group A streptococci using a phosphorylation-dependent
binding interaction between the response regulator CsrR and the
promoter region of the has operon.
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