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The c‐di‐GMP phosphodiesterase BifA regulates biofilm development in P seudomonas putida
Author(s) -
JiménezFernández Alicia,
LópezSánchez Aroa,
Calero Patricia,
Govantes Fernando
Publication year - 2015
Publication title -
environmental microbiology reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.229
H-Index - 69
ISSN - 1758-2229
DOI - 10.1111/1758-2229.12153
Subject(s) - biofilm , mutant , phosphodiesterase , chemistry , microbiology and biotechnology , biology , biochemistry , gene , bacteria , genetics , enzyme
Summary We previously showed the isolation of biofilm‐persistent P seudomonas putida mutants that fail to undergo biofilm dispersal upon entry in stationary phase. Two such mutants were found to bear insertions in PP 0914, encoding a GGDEF/EAL domain protein with high similarity to P seudomonas aeruginosa BifA . Here we show the phenotypic characterization of a Δ bifA mutant in P . putida KT 2442. This mutant displayed increased biofilm and pellicle formation, cell aggregation in liquid medium and decreased starvation‐induced biofilm dispersal relative to the wild type. Unlike its P . aeruginosa counterpart, P . putida BifA did not affect swarming motility. The hyperadherent phenotype of the Δ bifA mutant correlates with a general increase in cyclic diguanylate ( c‐di‐GMP ) levels, C ongo Red‐binding exopolysaccharide production and transcription of the adhesin‐encoding lapA gene. Integrity of the EAL motif and a modified GGDEF motif (altered to GGDQF ) were crucial for BifA activity, and c‐di‐GMP depletion by overexpression of a heterologous c‐di‐GMP phosphodiesterase in the Δ bifA mutant restored wild‐type biofilm dispersal and lapA expression. Our results indicate that BifA is a phosphodiesterase involved in the regulation of the c‐di‐GMP pool and required for the generation of the low c‐di‐GMP signal that triggers starvation‐induced biofilm dispersal.