Document Detail


Synthesis and Characterization of a Fluorescent Analogue of Cyclic-di-GMP.
MedLine Citation:
PMID:  22715917     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Cyclic-di-GMP, a ubiquitous bacterial second messenger has emerged as a key controller of several biological processes. Numbers of reports have appeared in the literatures which deal with the mechanistic aspects of this second messenger. However, the lack of a reporter tag attached to the c-di-GMP at times would limit the understandings of further details. In this study, we have chemically coupled N-Methylisatoic anhydride (MANT) with c-di-GMP giving rise to Mant-(c-di-GMP) or MANT-CDG. We have characterized the chemical and physical properties, and spectral behaviour of MANT-CDG. Fluorescence of MANT-CDG is sensitive to the change in the microenvironment, which helped us to study its interaction with three different c-di-GMP binding proteins (a diguanylate cyclase, a phosphodiesterase and a PilZ domain containing protein). In addition, we have shown here that MANT-CDG can inhibit diguanylate cyclase activity; however, it gets hydrolyzed by c-di-GMP specific phosphodiesterase. Taken together, our data suggest that MANT-CDG behaves similar to the native c-di-GMP and this study raises the possibility that MANT-CDG will be a valuable research tool for in vitro characterization of c-di-GMP signaling factors.
Authors:
Indra Mani Sharma; Thillaivillalan Dhanaraman; Ritta Mathew; Dipankar Chatterji
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-6-20
Journal Detail:
Title:  Biochemistry     Volume:  -     ISSN:  1520-4995     ISO Abbreviation:  -     Publication Date:  2012 Jun 
Date Detail:
Created Date:  2012-6-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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