期刊
FEMS MICROBIOLOGY LETTERS
卷 247, 期 2, 页码 123-130出版社
OXFORD UNIV PRESS
DOI: 10.1016/j.femsle.2005.04.036
关键词
EAL domain; phosphodiesterase; cyclic-di-GMP; bis-pNPP; biofilm formation; Yersinia pestis
类别
资金
- NIAID NIH HHS [AI25098] Funding Source: Medline
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-pNPP) 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. (c) 2005 Federation of European Microbiological Societies. Published by Elsevier B.V. All rights reserved.
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