scholarly journals Formation of a complex between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Shi-qi An ◽  
Ji-liang Tang
Keyword(s):  
Virulence Factors ◽  
Xanthomonas Campestris ◽  
Adaptor Protein ◽  
Physical Interaction ◽  
Diguanylate Cyclase ◽  
Domain Interaction ◽  
Ggdef Domain ◽  
Interdomain Interactions ◽  
Xanthomonas Campestris Pv Campestris ◽  
Two Hybrid

RpfG is a member of a class of wide spread bacterial two-component regulators with an HD-GYP cyclic di-GMP phosphodiesterase domain. In the plant pathogen Xanthomonas campestris pv. campestris (Xcc), RpfG together with the sensor kinase RpfC regulates the synthesis of a range of virulence factors as a response to the cell-cell Diffusible Signaling Factor (DSF). RpfG regulates many different virulence factors by divergent pathways. Physical interaction of RpfG with two diguanylate cyclase (GGDEF) domain proteins controls motility. This is a dynamic interaction that depends upon DSF signaling and involves the conserved GYP motif in the HD-GYP domain. Here we use synthetic peptide overlay technology and yeast two-hybrid analysis in conjunction with alanine substitution mutagenesis to define a motif within the GGDEF domain proteins required for interaction. We show that regulation of motility by the GGDEF domain proteins depends upon this motif. Furthermore, we show by Y2H that both GGDEF domain proteins bind a specific PilZ domain adaptor protein, and this interacts with the pilus motor proteins PilU and PiIT. The results support a model in which DSF signaling influences motility through the interaction of proteins that affect pilus action. The motif required for HD-GYP domain interaction is conserved in a number of GGDEF domain proteins, suggesting that regulation via interdomain interactions may be of broad relevance.

scholarly journals Requirement of a mip-Like Gene for Virulence in the Phytopathogenic Bacterium Xanthomonas campestris pv. campestris

2007 ◽  
Vol 20 (1) ◽  
pp. 21-30 ◽  
Author(s):  
Ning Zang ◽  
Dong-Jie Tang ◽  
Mei-Liang Wei ◽  
Yong-Qiang He ◽  
Baoshan Chen ◽  
...  
Keyword(s):  
Virulence Factors ◽  
Legionella Pneumophila ◽  
Xanthomonas Campestris ◽  
Bacterial Pathogen ◽  
Replication Capacity ◽  
Human Pathogens ◽  
Extracellular Proteases ◽  
Ppiase Activity ◽  
Phytopathogenic Bacterium ◽  
Xanthomonas Campestris Pv Campestris

Macrophage infectivity potentiators (Mips) are FKBP domain-containing proteins reported as virulence factors in several human pathogens, such as members of genera Legionella, Salmonella and Chlamydia. The putative peptidyl-prolyl cis-trans isomerase (PPIase) encoded by XC2699 of the plant bacterial pathogen Xanthomonas campestris pv. campestris 8004 exhibits a 49% similarity at the aminoacid level to the Mip protein of Legionella pneumophila. This mip-like gene, XC2699, was overexpressed in Es-cherichia coli and the purified (His)6-tagged Mip-like protein encoded by XC2699 exhibited a PPIase activity specifically inhibited by FK-506. A mutation in the mip-like gene XC2699 led to significant reductions in virulence and replication capacity in the host plant Chinese radish (Raphanus sativus L. var. radiculus Pers.). Furthermore, the production of exopolysaccharide and the activity of extracellular proteases, virulence factors X. campestris pv. campestris, were significantly decreased in the mip-like mutant. These results reveal that the mip-like gene is involved in the pathogenesis of X. campestris pv. campestris through an effect on the production of these virulence factors.

BIOCHEMICAL IDENTIFICATION OF PATOVARS OF THE PATHOGEN OF VASCULAR BACTERIOSIS OF THE CRUCIFEROUS XANTHOMONAS CAMPESTRIS PV. CAMPESTRIS

2020 ◽  
Vol 15 (1) ◽  
pp. 82-88
Author(s):  
Mikhail Kuznetsov ◽  
◽  
Anatoly Scherbakov ◽  
Elena Gorelnikova ◽  
Nadezhda Chervyakova ◽  
...  
Keyword(s):  
Xanthomonas Campestris ◽  
Biochemical Identification ◽  
Xanthomonas Campestris Pv Campestris

Survival of Xanthomonas campestris pv. campestris in the phyllosphere and rhizosphere of crops

2021 ◽  
Author(s):  
João César da Silva ◽  
Tadeu Antônio Fernandes da Silva Júnior ◽  
José Marcelo Soman ◽  
Daniele Maria do Nascimento ◽  
Luana Laurindo de Melo ◽  
...  
Keyword(s):  
Xanthomonas Campestris ◽  
Xanthomonas Campestris Pv Campestris

scholarly journals Genomic insights advance the fight against black rot of crucifers

2021 ◽  
Vol 87 (3) ◽  
pp. 127-136
Author(s):  
Zoë E. Dubrow ◽  
Adam J. Bogdanove
Keyword(s):  
Virulence Factors ◽  
Xanthomonas Campestris ◽  
Plant Pathogens ◽  
Impact Resistance ◽  
Resistance Breeding ◽  
Genetic Data ◽  
Black Rot ◽  
Inoculum Sources ◽  
New Knowledge ◽  
The World

AbstractXanthomonas campestris pv. campestris, the causal agent of black rot of crucifers, was one of the first bacterial plant pathogens ever identified. Over 130 years later, black rot remains a threat to cabbage, cauliflower, and other Brassica crops around the world. Recent genomic and genetic data are informing our understanding of X. campestris taxonomy, dissemination, inoculum sources, and virulence factors. This new knowledge promises to positively impact resistance breeding of Brassica varieties and management of inoculum sources.

Silver nanoparticles eliminate Xanthomonas campestris pv. campestris in cabbage seeds more efficiently than hot water treatment

2021 ◽  
Vol 27 ◽  
pp. 102284
Author(s):  
Jakub Pečenka ◽  
Zuzana Bytešníková ◽  
Tomáš Kiss ◽  
Eliška Peňázová ◽  
Miroslav Baránek ◽  
...  
Keyword(s):  
Silver Nanoparticles ◽  
Water Treatment ◽  
Xanthomonas Campestris ◽  
Hot Water ◽  
Hot Water Treatment ◽  
Xanthomonas Campestris Pv Campestris

scholarly journals A Novel Human Ada2 Homologue Functions with Gcn5 or Brg1 To Coactivate Transcription

2003 ◽  
Vol 23 (19) ◽  
pp. 6944-6957 ◽  
Author(s):  
Nickolai A. Barlev ◽  
Alexander V. Emelyanov ◽  
Paola Castagnino ◽  
Philip Zegerman ◽  
Andrew J. Bannister ◽  
...  
Keyword(s):  
Histone Acetylation ◽  
Chromatin Remodeling ◽  
Adaptor Protein ◽  
Saga Complex ◽  
Yeast Two Hybrid ◽  
Functional Assays ◽  
Two Hybrid ◽  
Histone Acetyltransferase Activity

ABSTRACT In yeast, the transcriptional adaptor yeast Ada2 (yAda2) is a part of the multicomponent SAGA complex, which possesses histone acetyltransferase activity through action of the yGcn5 catalytic enzyme. yAda2, among several SAGA proteins, serves to recruit SAGA to genes via interactions with promoter-bound transcription factors. Here we report identification of a new human Ada2 homologue, hAda2β. Ada2β differs both biochemically and functionally from the previously characterized hAda2α, which is a stable component of the human PCAF (human Gcn5 homologue) acetylase complex. Ada2β, relative to Ada2α, interacted selectively, although not stably, with the Gcn5-containing histone acetylation complex TFTC/STAGA. In addition, Ada2β interacted with Baf57 (a component of the human Swi/Snf complex) in a yeast two-hybrid screen and associated with human Swi/Snf in vitro. In functional assays, hAda2β (but not Ada2α), working in concert with Gcn5 (but not PCAF) or Brg1 (the catalytic component of hSwi/Snf complex), increased transcription via the B-cell-specific transcription factor Pax5/BSAP. These findings support the view that Gcn5 and PCAF have distinct roles in vivo and suggest a new mechanism of coactivator function, in which a single adaptor protein (Ada2β) can coordinate targeting of both histone acetylation and chromatin remodeling activities.

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