Comparative genomics of cyclic-di-GMP signalling in bacteria: post-translational regulation and catalytic activity.

ABSTRACT: Cyclic-di-GMP is a bacterial second messenger that controls the switch between motile and sessile states. It is synthesized by proteins containing the enzymatic GGDEF domain and degraded by the EAL domain. Many bacterial genomes encode several copies of proteins containing these domains, raising questions on how the activities of parallel c-di-GMP signalling systems are segregated to avoid potentially deleterious cross-talk. Moreover, many 'hybrid' proteins contain both GGDEF and EAL domains; the relationship between the two apparently opposing enzymatic activities has been termed a 'biochemical conundrum'. Here, we present a computational analysis of 11 248 GGDEF- and EAL-containing proteins in 867 prokaryotic genomes to address these two outstanding questions. Over half of these proteins

SUBMITTER: Seshasayee AS 

PROVIDER: S-EPMC2952852 | biostudies-literature | 2010 Oct

REPOSITORIES: biostudies-literature