rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 2
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pubmed:dateCreated |
2007-1-29
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pubmed:abstractText |
SET domain genes have been identified in numbers of bacterial genomes based on similarity to SET domains of eukaryotic histone methyltransferases. Herein, a Chlamydophila pneumoniae SET domain gene was clarified to be coincidently expressed with hctA and hctB genes encoding chlamydial histone H1-like proteins, Hc1 and Hc2, respectively. The SET domain protein (cpnSET) is localized in chlamydial cells and interacts with Hc1 and Hc2 through the C-terminal SET domain. As expected from conservation of catalytic sites in cpnSET, it functions as a protein methyltransferase to murine histone H3 and Hc1. However, little is known about protein methylation in the molecular pathogenesis of chlamydial infection. cpnSET may play an important role in chlamydial cell maturation due to modification of chlamydial histone H1-like proteins.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hc1 protein, Chlamydia trachomatis,
http://linkedlifedata.com/resource/pubmed/chemical/HctB protein, Chlamydia trachomatis,
http://linkedlifedata.com/resource/pubmed/chemical/Histone-Lysine N-Methyltransferase,
http://linkedlifedata.com/resource/pubmed/chemical/Histones,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Methyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/histone methyltransferase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1350-0872
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
153
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
585-92
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:17259630-Amino Acid Sequence,
pubmed-meshheading:17259630-Animals,
pubmed-meshheading:17259630-Bacterial Proteins,
pubmed-meshheading:17259630-Cell Line,
pubmed-meshheading:17259630-Chlamydophila pneumoniae,
pubmed-meshheading:17259630-DNA-Binding Proteins,
pubmed-meshheading:17259630-Histone-Lysine N-Methyltransferase,
pubmed-meshheading:17259630-Histones,
pubmed-meshheading:17259630-Humans,
pubmed-meshheading:17259630-Mice,
pubmed-meshheading:17259630-Molecular Sequence Data,
pubmed-meshheading:17259630-Protein Methyltransferases,
pubmed-meshheading:17259630-Protozoan Proteins,
pubmed-meshheading:17259630-RNA-Binding Proteins,
pubmed-meshheading:17259630-Two-Hybrid System Techniques
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pubmed:year |
2007
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pubmed:articleTitle |
Chlamydial SET domain protein functions as a histone methyltransferase.
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pubmed:affiliation |
Department of Microbiology and Immunology, Yamaguchi University School of Medicine, 1-1-1 Minami-Kogushi, Ube, Yamaguchi 755-8505, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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