scholarly journals A protein secretion system linked to bacteroidete gliding motility and pathogenesis

2009 ◽  
Vol 107 (1) ◽  
pp. 276-281 ◽  
Author(s):  
K. Sato ◽  
M. Naito ◽  
H. Yukitake ◽  
H. Hirakawa ◽  
M. Shoji ◽  
...  
Keyword(s):  
Protein Secretion ◽  
Secretion System ◽  
Gliding Motility ◽  
Protein Secretion System

scholarly journals Untangling Flavobacterium johnsoniae Gliding Motility and Protein Secretion

2017 ◽  
Vol 200 (2) ◽  
Author(s):  
Joseph J. Johnston ◽  
Abhishek Shrivastava ◽  
Mark J. McBride
Keyword(s):  
Amino Acids ◽  
Protein Secretion ◽  
Secretion System ◽  
Gliding Motility ◽  
Content Type ◽  
Flavobacterium Johnsoniae ◽  
C Terminus ◽  
Genes Encoding ◽  
Surface Localization ◽  
Protein Secretion System

ABSTRACTFlavobacterium johnsoniaeexhibits rapid gliding motility over surfaces. At least 20 genes are involved in this process. Seven of these,gldK,gldL,gldM,gldN,sprA,sprE, andsprT, encode proteins of the type IX protein secretion system (T9SS). The T9SS is required for surface localization of the motility adhesins SprB and RemA, and for secretion of the soluble chitinase ChiA. Here, we demonstrate that the gliding motility proteins GldA, GldB, GldD, GldF, GldH, GldI, and GldJ are also essential for secretion. Cells with mutations in the genes encoding any of these seven proteins had normal levels ofgldKmRNA but dramatically reduced levels of the GldK protein, which may explain the secretion defects of the motility mutants. GldJ is necessary for stable accumulation of GldK, and each mutant lacked the GldJ protein.F. johnsoniaecells that produced truncated GldJ, lacking eight to 13 amino acids from the C terminus, accumulated GldK but were deficient in gliding motility. SprB was secreted by these cells but was not propelled along their surfaces. This C-terminal region of GldJ is thus required for gliding motility but not for secretion. The identification of mutants that are defective for motility but competent for secretion begins to untangle theF. johnsoniaegliding motility machinery from the T9SS.IMPORTANCEMany members of the phylumBacteroidetessecrete proteins using T9SSs. T9SSs appear to be confined to members of this phylum. Many of these bacteria also glide rapidly over surfaces using a motility machine that is also confined to theBacteroidetesand appears to be intertwined with the T9SS. This study identifiesF. johnsoniaeproteins that are required for both T9SS function and gliding motility. It also provides an explanation for the link between secretion and gliding and identifies mutants with defects in motility but not secretion.

scholarly journals Genome Sequence of Flavobacteriaceae Strain W22, Isolated from a Tree Hole Mosquito Habitat

2020 ◽  
Vol 9 (7) ◽  
Author(s):  
Shicheng Chen ◽  
Edward D. Walker
Keyword(s):  
Protein Secretion ◽  
Draft Genome ◽  
Larval Habitat ◽  
Secretion System ◽  
Gliding Motility ◽  
Content Type ◽  
Polysaccharide Degradation ◽  
Tree Hole ◽  
Genes Encoding ◽  
Protein Secretion System

The bacterium Flavobacteriaceae strain W22 was isolated from the water column of a tree hole larval habitat of the mosquito Aedes triseriatus. The draft genome contained 3,796,379 bp, a G+C content of 35.4%, and several genes encoding enzymes functioning in polysaccharide degradation, gliding motility, and the type IX protein secretion system (T9SS).

scholarly journals Gliding Motility and Por Secretion System Genes Are Widespread among Members of the Phylum Bacteroidetes

2012 ◽  
Vol 195 (2) ◽  
pp. 270-278 ◽  
Author(s):  
Mark J. McBride ◽  
Yongtao Zhu
Keyword(s):  
Protein Secretion ◽  
Secretion System ◽  
Gliding Motility ◽  
Secretion Systems ◽  
Content Type ◽  
Flavobacterium Johnsoniae ◽  
Protein Secretion System ◽  
Gliding Bacterium ◽  
Protein Secretion Systems ◽  
Bacterial Secretion

ABSTRACTThe phylumBacteroidetesis large and diverse, with rapid gliding motility and the ability to digest macromolecules associated with many genera and species. Recently, a novel protein secretion system, the Por secretion system (PorSS), was identified in two members of the phylum, the gliding bacteriumFlavobacterium johnsoniaeand the nonmotile oral pathogenPorphyromonas gingivalis. The components of the PorSS are not similar in sequence to those of other well-studied bacterial secretion systems. TheF. johnsoniaePorSS genes are a subset of the gliding motility genes, suggesting a role for the secretion system in motility. TheF. johnsoniaePorSS is needed for assembly of the gliding motility apparatus and for secretion of a chitinase, and theP. gingivalisPorSS is involved in secretion of gingipain protease virulence factors. Comparative analysis of 37 genomes of members of the phylumBacteroidetesrevealed the widespread occurrence of gliding motility genes and PorSS genes. Genes associated with other bacterial protein secretion systems were less common. The results suggest that gliding motility is more common than previously reported. Microscopic observations confirmed that organisms previously described as nonmotile, includingCroceibacter atlanticus, “Gramella forsetii,”Paludibacter propionicigenes,Riemerella anatipestifer, andRobiginitalea biformata, exhibit gliding motility. Three genes (gldA,gldF, andgldG) that encode an apparent ATP-binding cassette transporter required forF. johnsoniaegliding were absent from two related gliding bacteria, suggesting that the transporter may not be central to gliding motility.

scholarly journals A holin/peptidoglycan hydrolase‐dependent protein secretion system

2020 ◽  
Author(s):  
Tracy Palmer ◽  
Alexander J. Finney ◽  
Chayan Kumar Saha ◽  
Gemma C. Atkinson ◽  
Frank Sargent
Keyword(s):  
Protein Secretion ◽  
Secretion System ◽  
Peptidoglycan Hydrolase ◽  
Protein Secretion System ◽  
Dependent Protein

scholarly journals PopF1 and PopF2, Two Proteins Secreted by the Type III Protein Secretion System of Ralstonia solanacearum, Are Translocators Belonging to the HrpF/NopX Family

2006 ◽  
Vol 188 (13) ◽  
pp. 4903-4917 ◽  
Author(s):  
Damien Meyer ◽  
Sébastien Cunnac ◽  
Mareva Guéneron ◽  
Céline Declercq ◽  
Frédérique Van Gijsegem ◽  
...  
Keyword(s):  
Protein Secretion ◽  
Ralstonia Solanacearum ◽  
Xanthomonas Campestris ◽  
Pathogenic Bacteria ◽  
Secretion System ◽  
Effector Proteins ◽  
Experimental Conditions ◽  
Type Iii ◽  
Protein Secretion System ◽  
Type Iii Protein Secretion

ABSTRACT Ralstonia solanacearum GMI1000 is a gram-negative plant pathogen which contains an hrp gene cluster which codes for a type III protein secretion system (TTSS). We identified two novel Hrp-secreted proteins, called PopF1 and PopF2, which display similarity to one another and to putative TTSS translocators, HrpF and NopX, from Xanthomonas spp. and rhizobia, respectively. They also show similarities with TTSS translocators of the YopB family from animal-pathogenic bacteria. Both popF1 and popF2 belong to the HrpB regulon and are required for the interaction with plants, but PopF1 seems to play a more important role in virulence and hypersensitive response (HR) elicitation than PopF2 under our experimental conditions. PopF1 and PopF2 are not necessary for the secretion of effector proteins, but they are required for the translocation of AvrA avirulence protein into tobacco cells. We conclude that PopF1 and PopF2 are type III translocators belonging to the HrpF/NopX family. The hrpF gene of Xanthomonas campestris pv. campestris partially restored HR-inducing ability to popF1 popF2 mutants of R. solanacearum, suggesting that translocators of R. solanacearum and Xanthomonas are functionally conserved. Finally, R. solanacearum strain UW551, which does not belong to the same phylotype as GMI1000, also possesses two putative translocator proteins. However, although one of these proteins is clearly related to PopF1 and PopF2, the other seems to be different and related to NopX proteins, thus showing that translocators might be variable in R. solanacearum.

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