Characterization of starvation-induced dispersion in Pseudomonas putida biofilms: genetic elements and molecular mechanisms

TY - JOUR

T1 - Characterization of starvation-induced dispersion in Pseudomonas putida biofilms: genetic elements and molecular mechanisms

AU - Gjermansen, Morten

AU - Nilsson, Martin

AU - Yang, Liang

AU - Tolker-Nielsen, Tim

PY - 2010/2

Y1 - 2010/2

N2 - Pseudomonas putida OUS82 biofilm dispersal was previously shown to be dependent on the gene PP0164 (here designated lapG). Sequence and structural analysis has suggested that the LapG geneproduct belongs to a family of cysteine proteinases that function in the modification of bacterial surface proteins. We provide evidence that LapG is involved in P. putida OUS82 biofilm dispersal through modification of the outer membrane-associated protein LapA. While the P. putida lapG mutant formed more biofilm than the wild-type, P. putida lapA and P. putida lapAG mutants displayed decreased surface adhesion and were deficient in subsequent biofilm formation, suggesting that LapG affects LapA, and that the LapA protein functions both as a surface adhesin and as a biofilm matrix component. Lowering of the intracellular c-di-GMP level via induction of an EAL domain protein led to dispersal of P. putida wild-type biofilm but did not disperse P. putida lapG biofilm, indicating that LapG exerts its activity on LapA in response to a decrease in the intracellular c-di-GMP level. In addition, evidence is provided that associated to LapA a cellulase-degradable exopolysaccharide is part of the P. putida biofilm matrix.

AB - Pseudomonas putida OUS82 biofilm dispersal was previously shown to be dependent on the gene PP0164 (here designated lapG). Sequence and structural analysis has suggested that the LapG geneproduct belongs to a family of cysteine proteinases that function in the modification of bacterial surface proteins. We provide evidence that LapG is involved in P. putida OUS82 biofilm dispersal through modification of the outer membrane-associated protein LapA. While the P. putida lapG mutant formed more biofilm than the wild-type, P. putida lapA and P. putida lapAG mutants displayed decreased surface adhesion and were deficient in subsequent biofilm formation, suggesting that LapG affects LapA, and that the LapA protein functions both as a surface adhesin and as a biofilm matrix component. Lowering of the intracellular c-di-GMP level via induction of an EAL domain protein led to dispersal of P. putida wild-type biofilm but did not disperse P. putida lapG biofilm, indicating that LapG exerts its activity on LapA in response to a decrease in the intracellular c-di-GMP level. In addition, evidence is provided that associated to LapA a cellulase-degradable exopolysaccharide is part of the P. putida biofilm matrix.

U2 - 10.1111/j.1365-2958.2009.06793.x

DO - 10.1111/j.1365-2958.2009.06793.x

M3 - Journal article

C2 - 19602146

SN - 0950-382X

VL - 75

SP - 815

EP - 826

JO - Molecular Microbiology

JF - Molecular Microbiology

IS - 4

ER -