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rdf:type |
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lifeskim:mentions |
umls-concept:C0032868,
umls-concept:C0043442,
umls-concept:C0205147,
umls-concept:C0441655,
umls-concept:C0919262,
umls-concept:C1514562,
umls-concept:C1880022,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2003941
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pubmed:issue |
22
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pubmed:dateCreated |
2008-1-4
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pubmed:abstractText |
The E3L gene is essential for pathogenesis in vaccinia virus. The E3L gene product consists of an N-terminal Z alpha domain and a C-terminal double-stranded RNA (dsRNA) binding domain; the left-handed Z-DNA-binding activity of the Z alpha domain of E3L is required for viral pathogenicity in mice. E3L is highly conserved among poxviruses, including the smallpox virus, and it is likely that the orthologous Z alpha domains play similar roles. To better understand the biological function of E3L proteins, we have investigated the Z-DNA-binding behavior of five representative Z alpha domains from poxviruses. Using surface plasmon resonance (SPR), we have demonstrated that these viral Z alpha domains bind Z-DNA tightly. Ability of Z alpha(E3L) converting B-DNA to Z-DNA was measured by circular dichroism (CD). The extents to which these Z alphas can stabilize Z-DNA vary considerably. Mutational studies demonstrate that residues in the loop of the beta-wing play an important role in this stabilization. Notably the Z alpha domain of vaccinia E3L acquires ability to convert B-DNA to Z-DNA by mutating amino acid residues in this region. Differences in the host cells of the various poxviruses may require different abilities to stabilize Z-DNA; this may be reflected in the observed differences in behavior in these Zalpha proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-10364558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-10843996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-11134298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-11524677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-11752168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-12777633,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-1350676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-14757814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-14981270,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-15448208,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-15659550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-15738948,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-16126896,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-16448869,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-8099244,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-8337842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-9237992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-9434718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-9748339,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-9792841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-9819417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17984076-9915827
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
1362-4962
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
35
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7714-20
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17984076-Amino Acid Sequence,
pubmed-meshheading:17984076-Chordopoxvirinae,
pubmed-meshheading:17984076-DNA,
pubmed-meshheading:17984076-DNA, Z-Form,
pubmed-meshheading:17984076-DNA-Binding Proteins,
pubmed-meshheading:17984076-Lysine,
pubmed-meshheading:17984076-Molecular Sequence Data,
pubmed-meshheading:17984076-Mutation,
pubmed-meshheading:17984076-Protein Structure, Tertiary,
pubmed-meshheading:17984076-RNA-Binding Proteins,
pubmed-meshheading:17984076-Sequence Alignment,
pubmed-meshheading:17984076-Surface Plasmon Resonance,
pubmed-meshheading:17984076-Threonine,
pubmed-meshheading:17984076-Viral Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
Characterization of DNA-binding activity of Z alpha domains from poxviruses and the importance of the beta-wing regions in converting B-DNA to Z-DNA.
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pubmed:affiliation |
Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Korea.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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