A Component of the Xanthomonadaceae Type IV Secretion System Combines a VirB7 Motif with a N0 Domain Found in Outer Membrane Transport Proteins
Identifieur interne : 000D36 ( Ncbi/Curation ); précédent : 000D35; suivant : 000D37A Component of the Xanthomonadaceae Type IV Secretion System Combines a VirB7 Motif with a N0 Domain Found in Outer Membrane Transport Proteins
Auteurs : Diorge P. Souza ; Maxuel O. Andrade ; Cristina E. Alvarez-Martinez ; Guilherme M. Arantes ; Chuck S. Farah ; Roberto K. SalinasSource :
- PLoS Pathogens [ 1553-7366 ] ; 2011.
English descriptors
- KwdEn :
- Amino Acid Sequence, Bacterial Outer Membrane Proteins (chemistry), Bacterial Outer Membrane Proteins (genetics), Bacterial Outer Membrane Proteins (isolation & purification), Bacterial Outer Membrane Proteins (metabolism), Citrus sinensis (microbiology), Crystallography, X-Ray (methods), Genetic Complementation Test, Immunoblotting, Lipoproteins (chemistry), Lipoproteins (genetics), Lipoproteins (isolation & purification), Lipoproteins (metabolism), Magnetic Resonance Spectroscopy (methods), Membrane Transport Proteins (chemistry), Membrane Transport Proteins (genetics), Membrane Transport Proteins (isolation & purification), Membrane Transport Proteins (metabolism), Models, Molecular, Molecular Sequence Data, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Tertiary, Protein Transport, Sequence Alignment, Sequence Deletion, Spectrometry, Fluorescence, Virulence Factors (chemistry), Virulence Factors (genetics), Virulence Factors (metabolism), Xanthomonas (chemistry), Xanthomonas (genetics), Xanthomonas (metabolism).
- MESH :
- chemical , chemistry : Bacterial Outer Membrane Proteins, Lipoproteins, Membrane Transport Proteins, Virulence Factors.
- chemical , genetics : Bacterial Outer Membrane Proteins, Lipoproteins, Membrane Transport Proteins, Virulence Factors.
- chemical , isolation & purification : Bacterial Outer Membrane Proteins, Lipoproteins, Membrane Transport Proteins.
- chemical , metabolism : Bacterial Outer Membrane Proteins, Lipoproteins, Membrane Transport Proteins, Virulence Factors.
- chemistry : Xanthomonas.
- genetics : Xanthomonas.
- metabolism : Xanthomonas.
- methods : Crystallography, X-Ray, Magnetic Resonance Spectroscopy.
- microbiology : Citrus sinensis.
- Amino Acid Sequence, Genetic Complementation Test, Immunoblotting, Models, Molecular, Molecular Sequence Data, Protein Interaction Domains and Motifs, Protein Multimerization, Protein Structure, Tertiary, Protein Transport, Sequence Alignment, Sequence Deletion, Spectrometry, Fluorescence.
Abstract
Type IV secretion systems (T4SS) are used by Gram-negative bacteria to translocate protein and DNA substrates across the cell envelope and into target cells. Translocation across the outer membrane is achieved via a ringed tetradecameric outer membrane complex made up of a small VirB7 lipoprotein (normally 30 to 45 residues in the mature form) and the C-terminal domains of the VirB9 and VirB10 subunits. Several species from the genera of
Url:
DOI: 10.1371/journal.ppat.1002031
PubMed: 21589901
PubMed Central: 3093366
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PMC:3093366Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A Component of the Xanthomonadaceae Type IV Secretion System Combines a VirB7 Motif with a N0 Domain Found in Outer Membrane Transport Proteins</title>
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<author><name sortKey="Arantes, Guilherme M" sort="Arantes, Guilherme M" uniqKey="Arantes G" first="Guilherme M." last="Arantes">Guilherme M. Arantes</name>
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<series><title level="j">PLoS Pathogens</title>
<idno type="ISSN">1553-7366</idno>
<idno type="eISSN">1553-7374</idno>
<imprint><date when="2011">2011</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Bacterial Outer Membrane Proteins (chemistry)</term>
<term>Bacterial Outer Membrane Proteins (genetics)</term>
<term>Bacterial Outer Membrane Proteins (isolation & purification)</term>
<term>Bacterial Outer Membrane Proteins (metabolism)</term>
<term>Citrus sinensis (microbiology)</term>
<term>Crystallography, X-Ray (methods)</term>
<term>Genetic Complementation Test</term>
<term>Immunoblotting</term>
<term>Lipoproteins (chemistry)</term>
<term>Lipoproteins (genetics)</term>
<term>Lipoproteins (isolation & purification)</term>
<term>Lipoproteins (metabolism)</term>
<term>Magnetic Resonance Spectroscopy (methods)</term>
<term>Membrane Transport Proteins (chemistry)</term>
<term>Membrane Transport Proteins (genetics)</term>
<term>Membrane Transport Proteins (isolation & purification)</term>
<term>Membrane Transport Proteins (metabolism)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Tertiary</term>
<term>Protein Transport</term>
<term>Sequence Alignment</term>
<term>Sequence Deletion</term>
<term>Spectrometry, Fluorescence</term>
<term>Virulence Factors (chemistry)</term>
<term>Virulence Factors (genetics)</term>
<term>Virulence Factors (metabolism)</term>
<term>Xanthomonas (chemistry)</term>
<term>Xanthomonas (genetics)</term>
<term>Xanthomonas (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Bacterial Outer Membrane Proteins</term>
<term>Lipoproteins</term>
<term>Membrane Transport Proteins</term>
<term>Virulence Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Outer Membrane Proteins</term>
<term>Lipoproteins</term>
<term>Membrane Transport Proteins</term>
<term>Virulence Factors</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Bacterial Outer Membrane Proteins</term>
<term>Lipoproteins</term>
<term>Membrane Transport Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Outer Membrane Proteins</term>
<term>Lipoproteins</term>
<term>Membrane Transport Proteins</term>
<term>Virulence Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Xanthomonas</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Xanthomonas</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Xanthomonas</term>
</keywords>
<keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Crystallography, X-Ray</term>
<term>Magnetic Resonance Spectroscopy</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Citrus sinensis</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Genetic Complementation Test</term>
<term>Immunoblotting</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Interaction Domains and Motifs</term>
<term>Protein Multimerization</term>
<term>Protein Structure, Tertiary</term>
<term>Protein Transport</term>
<term>Sequence Alignment</term>
<term>Sequence Deletion</term>
<term>Spectrometry, Fluorescence</term>
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<front><div type="abstract" xml:lang="en"><p>Type IV secretion systems (T4SS) are used by Gram-negative bacteria to translocate protein and DNA substrates across the cell envelope and into target cells. Translocation across the outer membrane is achieved via a ringed tetradecameric outer membrane complex made up of a small VirB7 lipoprotein (normally 30 to 45 residues in the mature form) and the C-terminal domains of the VirB9 and VirB10 subunits. Several species from the genera of <italic>Xanthomonas</italic>
phytopathogens possess an uncharacterized type IV secretion system with some distinguishing features, one of which is an unusually large VirB7 subunit (118 residues in the mature form). Here, we report the NMR and 1.0 Å X-ray structures of the VirB7 subunit from <italic>Xanthomonas citri</italic>
subsp. citri (VirB7<sub>XAC2622</sub>
) and its interaction with VirB9. NMR solution studies show that residues 27–41 of the disordered flexible N-terminal region of VirB7<sub>XAC2622</sub>
interact specifically with the VirB9 C-terminal domain, resulting in a significant reduction in the conformational freedom of both regions. VirB7<sub>XAC2622</sub>
has a unique C-terminal domain whose topology is strikingly similar to that of N0 domains found in proteins from different systems involved in transport across the bacterial outer membrane. We show that VirB7<sub>XAC2622</sub>
oligomerizes through interactions involving conserved residues in the N0 domain and residues 42–49 within the flexible N-terminal region and that these homotropic interactions can persist in the presence of heterotropic interactions with VirB9. Finally, we propose that VirB7<sub>XAC2622</sub>
oligomerization is compatible with the core complex structure in a manner such that the N0 domains form an extra layer on the perimeter of the tetradecameric ring.</p>
</div>
</front>
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