Identification and characterization of the biochemical function of <i><scp>A</scp>grobacterium </i><scp>T</scp>‐complex‐recruiting protein <scp>A</scp>tu5117

Gao, Dian-Kun; Bian, Xiaowei; Guo, Minliang; Wang, Jing; Zhang, Xin

doi:10.1111/febs.12460

Cited by 5 publications

(3 citation statements)

References 42 publications

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“…Associated functional studies of the HEPN domain of VBP have demonstrated that the dimerization of VBP is essential for the induction of tumors in plants ( Padavannil et al, 2014 ). Our recent experimental data confirmed that VBP1 (encoded by atu5117 ) is an NTPase that might energize the recruitment of T-complex to the transport site ( Gao et al, 2013 ).…”

Section: Introductionsupporting

confidence: 58%

“…Bioinformatics investigations have demonstrated that three VBPs are highly conversed with regard to their functional domains, and all of the VBPs contain a putative nucleotidyltransferase domain near the N-terminus and a putative higher eukaryotes and prokaryotes nucleotide-binding (HEPN) domain near the C-terminus ( Guo et al, 2007b ; Gao et al, 2013 ). Structural studies have shown that VBP is a dimer and that the C-terminal HEPN domain is the dimerization domain of VBP.…”

Section: Introductionmentioning

confidence: 99%

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Expression of Agrobacterium Homolog Genes Encoding T-complex Recruiting Protein under Virulence Induction Conditions

Yang

Zhang

et al. 2015

Front. Microbiol.

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The proteins encoded by three Agrobacterial genes, atu5117, atu4860, and atu4856, are highly homologous to each other in amino acid sequence. All three proteins can bind to VirD2 and are named VBP1, VBP2, and VBP3 (VirD2-binding protein), respectively. VBP is involved in T-DNA transfer by recruiting the T-complex from the cytosol to the polar transport apparatus T4SS (type IV secretion system) and is defined as the “T-complex recruiting protein.” However, it remains unknown how these three homologous genes co-exist in a relatively small prokaryotic genome. To understand whether these three homologous genes are expressed differentially under virulence induction conditions, we examined the effects of virulence induction conditions, including various pH values, temperatures and acetosyringone (AS, an effective virulence inducer to Agrobacterium tumefaciens) concentrations, on the expression of the three VBP-encoding genes. Our data showed that vbp1 (atu5117) and vbp3 (atu4856) maintained constant expression under the tested induction conditions, whereas the expression of vbp2 (atu4860) was affected by the conditions. Culture conditions favorable to the expression of vbp2 differed from the reported induction conditions for other virulence proteins. In particular, the pH value was a crucial factor for the expression of vbp2. In addition, the deletion of vbp1 affected the expression of vbp2. Taken together, these results suggest that the mechanisms regulating the expression of these three homologous genes are different from the virulence induction mechanism and that VBP homologs are presumably involved in other biological processes in addition to T-complex recruitment.

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Section: Introductionsupporting

confidence: 58%

Section: Introductionmentioning

confidence: 99%

Expression of Agrobacterium Homolog Genes Encoding T-complex Recruiting Protein under Virulence Induction Conditions

Yang

Zhang

et al. 2015

Front. Microbiol.

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“…Electrophoresis and immunoblotting analyses were carried out as described before [ 27 , 40 ]. Equal volumes (10 μL) of various samples were loaded for SDS-PAGE.…”

Section: Methodsmentioning

confidence: 99%

The Divergent Key Residues of Two Agrobacterium fabrum (tumefaciens) CheY Paralogs Play a Key Role in Distinguishing Their Functions

et al. 2021

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The chemotactic response regulator CheY, when phosphorylated by the phosphoryl group from phosphorylated CheA, can bind to the motor switch complex to control the flagellar motor rotation. Agrobacterium fabrum (previous name: Agrobacterium tumefaciens), a phytopathogen, carries two paralogous cheY genes, cheY1 and cheY2. The functional difference of two paralogous CheYs remains unclear. Three cheY-deletion mutants were constructed to test the effects of two CheYs on the chemotaxis of A. fabrum. Phenotypes of three cheY-deletion mutants show that deletion of each cheY significantly affects the chemotactic response, but cheY2-deletion possesses more prominent effects on the chemotactic migration and swimming pattern of A. fabrum than does cheY1-deletion. CheA-dependent cellular localization of two CheY paralogs and in vitro pull-down of two CheY paralogs by FliM demonstrate that the distinct roles of two CheY paralogs arise mainly from the differentiation of their binding affinities for the motor switch component FliM, agreeing with the divergence of the key residues on the motor-binding surface involved in the interaction with FliM. The single respective replacements of key residues R93 and A109 on the motor-binding surface of CheY2 by alanine (A) and valine (V), the corresponding residues of CheY1, significantly enhanced the function of CheY2 in regulating the chemotactic response of A. fabrum CheY-deficient mutant Δy to nutrient substances and host attractants. These results conclude that the divergence of the key residues in the functional subdomain is the decisive factor of functional differentiation of these two CheY homologs and protein function may be improved by the substitution of the divergent key residues in the functional domain for the corresponding residues of its paralogs. This finding will help us to better understand how paralogous proteins sub-functionalize. In addition, the acquirement of two CheY2 variants, whose chemotactic response functions are significantly improved, will be very useful for us to further explore the mechanism of CheY to bind and regulate the flagellar motor and the role of chemotaxis in the pathogenicity of A. fabrum.

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Is there any crosstalk between the chemotaxis and virulence induction signaling in Agrobacterium tumefaciens ?

Guo

Huang

Yang

2017

Biotechnology Advances

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Identification and characterization of the biochemical function of Agrobacterium T‐complex‐recruiting protein Atu5117

Cited by 5 publications

References 42 publications

Expression of Agrobacterium Homolog Genes Encoding T-complex Recruiting Protein under Virulence Induction Conditions

Expression of Agrobacterium Homolog Genes Encoding T-complex Recruiting Protein under Virulence Induction Conditions

The Divergent Key Residues of Two Agrobacterium fabrum (tumefaciens) CheY Paralogs Play a Key Role in Distinguishing Their Functions

Is there any crosstalk between the chemotaxis and virulence induction signaling in Agrobacterium tumefaciens ?

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