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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2001-9-27
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pubmed:abstractText |
Rat Sm-20 is a homologue of the Caenorhabditis elegans gene egl-9 and has been implicated in the regulation of growth, differentiation and apoptosis in muscle and nerve cells. Null mutants in egl-9 result in a complete tolerance to an otherwise lethal toxin produced by Pseudomonas aeruginosa. This study describes the conserved Egl-Nine (EGLN) gene family of which rat SM-20 and C. elegans Egl-9 are members and characterizes the mouse and human homologues. Each of the human genes (EGLN1, EGLN2 and EGLN3) are of a conserved genomic structure consisting of five coding exons. Phylogenetic analysis and domain organization show that EGLN1 represents the ancestral form of the gene family and that EGLN3 is the human orthologue of rat Sm-20. The previously observed mitochondrial targeting of rat SM-20 is unlikely to be a general feature of the protein family and may be a feature specific to rats. An EGLN gene is unexpectedly found in the genome of P. aeruginosa, a bacterium known to produce a toxin that acts through the Egl-9 protein. The pathogenic bacterium Vibrio cholerae is also shown to have an EGLN gene suggesting that it is an important pathogenicity factor. These results provide new insights into host-pathogen interactions and a basis for further functional characterization of the gene family and resolve discrepancies in annotation between gene family members.
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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/Caenorhabditis elegans Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/EGLN1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Egl-9 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Egln1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Egln3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Procollagen-Proline Dioxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SCAND2 protein, human
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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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 |
5
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
125-32
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pubmed:dateRevised |
2007-9-25
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pubmed:meshHeading |
pubmed-meshheading:11574160-Amino Acid Sequence,
pubmed-meshheading:11574160-Animals,
pubmed-meshheading:11574160-Binding Sites,
pubmed-meshheading:11574160-Caenorhabditis elegans,
pubmed-meshheading:11574160-Caenorhabditis elegans Proteins,
pubmed-meshheading:11574160-Conserved Sequence,
pubmed-meshheading:11574160-DNA-Binding Proteins,
pubmed-meshheading:11574160-Databases, Nucleic Acid,
pubmed-meshheading:11574160-Evolution, Molecular,
pubmed-meshheading:11574160-Gene Transfer, Horizontal,
pubmed-meshheading:11574160-Helminth Proteins,
pubmed-meshheading:11574160-Humans,
pubmed-meshheading:11574160-Immediate-Early Proteins,
pubmed-meshheading:11574160-Mice,
pubmed-meshheading:11574160-Molecular Sequence Data,
pubmed-meshheading:11574160-Multigene Family,
pubmed-meshheading:11574160-Phylogeny,
pubmed-meshheading:11574160-Procollagen-Proline Dioxygenase,
pubmed-meshheading:11574160-Proteins,
pubmed-meshheading:11574160-Rats,
pubmed-meshheading:11574160-Sequence Alignment,
pubmed-meshheading:11574160-Sequence Homology, Amino Acid
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pubmed:year |
2001
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pubmed:articleTitle |
Characterization and comparative analysis of the EGLN gene family.
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pubmed:affiliation |
Medical Genetics Section, University of Edinburgh, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, UK. martin.taylor@ed.ac.uk
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pubmed:publicationType |
Journal Article,
Comparative Study
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