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Genetic dissection of a motility‐associated c‐di‐ GMP signalling protein of P seudomonas putida
Author(s) -
Österberg Sofia,
Åberg Anna,
Herrera Seitz M Karina,
WolfWatz Magnus,
Shingler Victoria
Publication year - 2013
Publication title -
environmental microbiology reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.229
H-Index - 69
ISSN - 1758-2229
DOI - 10.1111/1758-2229.12045
Subject(s) - pseudomonas putida , motility , second messenger system , biology , microbiology and biotechnology , mutant , biochemistry , phosphofructokinase 2 , effector , enzyme , chemistry , gene
Summary Lack of the P seudomonas putida PP 2258 protein or its overexpression results in defective motility on solid media. The PP 2258 protein is tripartite, possessing a PAS domain linked to two domains associated with turnover of c‐di‐ GMP – a cyclic nucleotide that controls the switch between motile and sessile lifestyles. The second messenger c‐di‐ GMP is produced by diguanylate cyclases and degraded by phosphodiesterases containing GGDEF and EAL or HD ‐ GYP domains respectively. It is common for enzymes involved in c‐di‐ GMP signalling to contain two domains with potentially opposing c‐di‐ GMP turnover activities; however, usually one is degenerate and has been adopted to serve regulatory functions. Only a few proteins have previously been found to have dual enzymatic activities – being capable of both synthesizing and hydrolysing c‐di‐ GMP . Here, using truncated and mutant derivatives of PP 2258, we show that despite a lack of complete consensus in either the GGDEF or EAL motifs, the two c‐di‐ GMP turnover domains can function independently of each other, and that the diguanylate cyclase activity is regulated by an inhibitory I ‐site within its GGDEF domain. Thus, motility‐associated PP 2258 can be added to the short list of bifunctional c‐di‐ GMP signalling proteins.