Yersinia pestis lacZ expresses a beta-galactosidase with low enzymatic activity.

Abstract:

:Although very little, if any, beta-galactosidase activity is detected in Yersinia pestis by a standard Miller assay, we found that Y. pestis KIM6+ cells formed blue colonies on plates containing 5-bromo-4-chloro-3-indolyl-beta-D-galactoside (X-gal). Searches of the Y. pestis genome databases revealed the presence of noncontiguous sequences highly homologous to Escherichia coli lacZ, lacY, and lacI. Yersinia pestis lacZ is predicted to encode a 1060 amino-acid protein with 62% identity and 72% similarity to beta-galactosidase from E. coli. A deletion in the Y. pestis lacZ gene caused the formation of white colonies on X-gal-containing plates and beta-galactosidase activity was at background levels in the KIM6+lacZ mutant, while the complemented strain expressed about 190 Miller units. The Y. pestis lacZ promoter was not regulated by isopropylthiogalactoside or glucose. Finally, uptake of lactose by Y. pestis may be impaired.

journal_name

FEMS Microbiol Lett

authors

Bobrov AG,Perry RD

doi

10.1111/j.1574-6968.2005.00039.x

keywords:

subject

Has Abstract

pub_date

2006-02-01 00:00:00

pages

43-51

issue

1

eissn

0378-1097

issn

1574-6968

pii

FML039

journal_volume

255

pub_type

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