Ha. Jones et al., HmsT, a protein essential for expression of the haemin storage (Hms(+)) phenotype of Yersinia pestis, MICROBIO-UK, 145, 1999, pp. 2117-2128
The haemin storage (Hms) phenotype of Yersinia pestis has been shown to be
involved in the blockage of fleas that is required for the transmission of
plague from fleas to mammals. Previously, an operon encoding four genes, hm
sHFRS, that are essential for the temperature-regulated Hms(+) phenotype ha
s been characterized. Here the isolation and characterization of a fifth ge
ne, hmsT, that is essential for this phenotype is described. Conceptual tra
nslation of hmsT suggests it encodes a 44.8 kDa protein with a pl of 7.75.
The gene for HmsT is located outside of the similar to 102 kb pgm locus of
Y. pestis that contains the hmsHFRS operon. Hybridization studies indicate
that Yersinia pseudotuberculosis but not Yersinia enterocolitica or Escheri
chia coli possesses a highly homologous gene. HmsT belongs to a family of P
leD-related proteins with four highly conserved regions of homology. Althou
gh PleD is a regulator, the functions of the other members of this family h
ave not been experimentally determined. The iron-responsive regulator, Fur,
has previously been implicated in temperature regulation of the Hms phenot
ype. A good potential Fur-binding site (FBS) is located upstream of hmsT. Y
. pestis M23 and two of five Y. pseudotuberculosis strains, which all exhib
it a temperature-constitutive Hms phenotype, contain a 6 bp insertion in th
e putative FBS. E. coli MG1655 contains homologues of hmsHFRST (ycdSRQPT) b
ut has an Hms(-) phenotype. Only ycdQ and ycdP complement mutations in thei
r respective homologues, hmsR and hmsS, in Y. pestis.