Dataset Information

Flagellin (FliC) phosphorylation affects Type 2 protease secretion and biofilm dispersal in Pseudomonas aeruginosa PAO1

ABSTRACT: Protein phosphorylation has a major role in controlling the life-cycle and infection stages of bacteria. Proteome-wide occurrence of S/T/Y phosphorylation has been reported for many prokaryotic systems. Previously, we reported the phosphoproteome of Pseudomonas aeruginosa and Pseudomonas putida. In this study, we show the role of S/T phosphorylation of one motility protein, FliC, in regulating multiple surface-associated phenomena of Pseudomonas aeruginosa PAO1. The absence of phosphorylation in the conserved T27 and S28 residues of flagellin FliC, interestingly, did not affect swimming motility, but affected the secretome of type 2 secretion system (T2SS) and biofilm formation of PAO1. Flagellin phosphomutants had increased levels and activities of type 2 secretome proteins. This occurs by a possible mechanism affecting the secretion efficiency of T2SS machinery. Flagellin phosphomutants also formed reduced biofilm at 24h and had delayed biofilm dispersal under static and dynamic flow conditions, respectively. The levels of type 2 secretome and biofilm formation under static conditions had an inverse correlation. Hence, increase in the levels of type 2 secretome was accompanied by reduced biofilm formation in the flagellin phosphomutants. Altogether, we found a system of phosphorylation that co-ordinately regulates surface related processes such as proteases secretion by T2SS, biofilm formation and dispersal.

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Pseudomonas Aeruginosa Pao1

SUBMITTER: Miao-Hsia Lin

LAB HEAD: Miao-Hsia Lin

PROVIDER: PXD003645 | Pride | 2022-03-02

REPOSITORIES: Pride

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			Action	DRS
	120714miao11_W_early.wiff	Wiff
	120714miao11_W_early.wiff.scan	Wiff
	120714miao14_W_late.wiff	Wiff
	120714miao14_W_late.wiff.scan	Wiff
	F001052.dat	Other

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Flagellin FliC Phosphorylation Affects Type 2 Protease Secretion and Biofilm Dispersal in Pseudomonas aeruginosa PAO1.

Suriyanarayanan Tanujaa T Periasamy Saravanan S Lin Miao-Hsia MH Ishihama Yasushi Y Swarup Sanjay S

PloS one 20161004 10

Protein phosphorylation has a major role in controlling the life-cycle and infection stages of bacteria. Proteome-wide occurrence of S/T/Y phosphorylation has been reported for many prokaryotic systems. Previously, we reported the phosphoproteome of Pseudomonas aeruginosa and Pseudomonas putida. In this study, we show the role of S/T phosphorylation of one motility protein, FliC, in regulating multiple surface-associated phenomena of P. aeruginosa PAO1. This is the first report of occurrence of ...[more]

PMID: 27701473

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