Source:http://linkedlifedata.com/resource/pubmed/id/12356262
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2002-10-1
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pubmed:abstractText |
SUMMARY Caenorhabditis elegans possesses two Notch-like receptors, LIN-12 and GLP-1, which have both overlapping and individual biological functions. We examined the lin-12 and glp-1 genes in closely related nematodes to learn about their evolution. Here we report molecular and functional analyses of lin-12 orthologs from two related nematodes, C. briggsae (Cb) and C. remanei (Cr). In addition, we compare these lin-12 findings with similar studies of Cb-glp-1 and Cr-glp-1 orthologs. Cb-LIN-12 and Cr-LIN-12 retain the same number and order of motifs as Ce-LIN-12. Intriguingly, we find that LIN-12 conservation differs from that of GLP-1 in two respects. First, individual motifs are conserved to a different degree for the two receptors. For example, the transmembrane domain is 16-32% identical among LIN-12 orthologs but 65-70% identical among GLP-1 orthologs. Second, certain amino acids are conserved in a receptor-specific manner, a phenomenon most prevalent in the CC-linker. We suggest that LIN-12 and GLP-1 have been molded by selective constraints that are receptor specific and that the two proteins may not be entirely interchangeable. To analyze the functions of the lin-12 orthologs, we used RNA-mediated interference (RNAi). Cb-lin-12(RNAi) or Cr-lin-12(RNAi) progeny are nearly 100% Lag, a larval lethality typical of C. elegans lin-12 glp-1 double mutants, but not the primary defect observed in Ce-lin-12 null mutants or Ce-lin-12(RNAi). Therefore, LIN-12 functions are similar, but not identical, among the Caenorhabditis species. We suggest that ancestral functions may have been divided between LIN-12 and GLP-1 receptors in a process contributing to the retention of both genes after gene duplication (i.e., subfunctionalization).
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pubmed:language |
eng
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pubmed:journal | |
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 Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lin-12 protein, C elegans,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:issn |
1520-541X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
319-33
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12356262-Amino Acid Sequence,
pubmed-meshheading:12356262-Animals,
pubmed-meshheading:12356262-Base Sequence,
pubmed-meshheading:12356262-Biological Evolution,
pubmed-meshheading:12356262-Blotting, Southern,
pubmed-meshheading:12356262-Caenorhabditis elegans,
pubmed-meshheading:12356262-Caenorhabditis elegans Proteins,
pubmed-meshheading:12356262-Cloning, Molecular,
pubmed-meshheading:12356262-DNA Primers,
pubmed-meshheading:12356262-Gene Duplication,
pubmed-meshheading:12356262-Helminth Proteins,
pubmed-meshheading:12356262-Membrane Proteins,
pubmed-meshheading:12356262-Molecular Sequence Data,
pubmed-meshheading:12356262-Phenotype,
pubmed-meshheading:12356262-Phylogeny,
pubmed-meshheading:12356262-RNA, Messenger,
pubmed-meshheading:12356262-Sequence Homology, Amino Acid
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pubmed:articleTitle |
Evolution of discrete Notch-like receptors from a distant gene duplication in Caenorhabditis.
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pubmed:affiliation |
Department of Biochemistry, University of Wisconsin-Madison, 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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