Open AccessThe phosphodiesterase activity of the HmsP EAL domain is required for negative regulation of biofilm formation in Yersinia pestis
Author(s) -
Bobrov Alexander G.,
Kirillina Olga,
Perry Robert D.
Publication year - 2005
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1016/j.femsle.2005.04.036
Subject(s) - yersinia pestis , phosphodiesterase , biofilm , chemistry , biochemistry , fusion protein , enzyme , recombinant dna , biology , bacteria , virulence , genetics , gene
In Yersinia pestis , biofilm formation is stimulated by HmsT, a GGDEF‐domain containing protein that synthesizes cyclic‐di‐GMP (c‐di‐GMP), and inhibited by HmsP, an EAL‐domain protein. Only the EAL‐domain portion of HmsP is required to inhibit biofilm formation. The EAL domain of HmsP was purified as a 6XHis‐tag fusion protein and demonstrated to have phosphodiesterase activity using bis( p ‐nitrophenyl) phosphate (bis‐ p NPP) as a substrate. This enzymatic activity was strictly manganese dependent. A critical residue (E506) of HmsP within the EAL domain, that is required for inhibition of biofilm formation, is also essential for this phosphodiesterase activity. While the proposed function of EAL‐domain proteins is to linearize c‐di‐GMP, this is a direct demonstration of the required phosphodiesterase activity of a purified EAL‐domain protein.