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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1-2
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pubmed:dateCreated |
2002-7-16
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pubmed:databankReference |
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pubmed:abstractText |
Three highly mutable loci of the wall-less pathogens Mycoplasma bovis, Mycoplasma pulmonis and Mycoplasma agalactiae undergo high-frequency genomic rearrangements and generate extensive antigenic variation of major surface lipoproteins. Adjacent to each locus, an open reading frame exists as a single chromosomal copy and is predicted to encode a site-specific DNA recombinase exhibiting high homology to the recombinases XerD of Escherichia coli and CodV of Bacillus subtilis. Each of the mycoplasmal proteins are members of the lambda integrase family of tyrosine site-specific recombinases and likely mediates site-specific DNA inversions observed within the adjacent, variable loci.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/AvgC protein, Anaplasma marginale,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Integrases,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinases,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Vsp protein, bacterial,
http://linkedlifedata.com/resource/pubmed/chemical/XerD protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
292
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
205-11
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12119115-Amino Acid Sequence,
pubmed-meshheading:12119115-Antigens, Bacterial,
pubmed-meshheading:12119115-Bacterial Outer Membrane Proteins,
pubmed-meshheading:12119115-Base Sequence,
pubmed-meshheading:12119115-Binding Sites,
pubmed-meshheading:12119115-Chromosome Mapping,
pubmed-meshheading:12119115-Cloning, Molecular,
pubmed-meshheading:12119115-DNA, Bacterial,
pubmed-meshheading:12119115-DNA Nucleotidyltransferases,
pubmed-meshheading:12119115-Escherichia coli Proteins,
pubmed-meshheading:12119115-Integrases,
pubmed-meshheading:12119115-Lipoproteins,
pubmed-meshheading:12119115-Molecular Sequence Data,
pubmed-meshheading:12119115-Mycoplasma,
pubmed-meshheading:12119115-Open Reading Frames,
pubmed-meshheading:12119115-Recombinases,
pubmed-meshheading:12119115-Sequence Alignment,
pubmed-meshheading:12119115-Sequence Analysis, DNA,
pubmed-meshheading:12119115-Sequence Homology, Amino Acid,
pubmed-meshheading:12119115-Sequence Homology, Nucleic Acid,
pubmed-meshheading:12119115-Species Specificity,
pubmed-meshheading:12119115-Tyrosine
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pubmed:year |
2002
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pubmed:articleTitle |
Identification and characterization of a site-specific tyrosine recombinase within the variable loci of Mycoplasma bovis, Mycoplasma pulmonis and Mycoplasma agalactiae.
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pubmed:affiliation |
Department of Membrane and Ultrastructure Research, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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