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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
|
| pubmed:dateCreated |
1995-9-8
|
| pubmed:databankReference | |
| pubmed:abstractText |
The mammalian low molecular mass protein-7 (LMP-7) gene resides in the class II region of the MHC, and its product is most probably involved, as a component of a proteasome, in the processing of Ags to be presented by the MHC class I molecules. To elucidate the evolution of the LMP-7 gene at both the primary structure and genetic levels, we isolated LMP-7 cDNA clones from amphibian Xenopus laevis, which last shared a common ancestor with mammals 350 x 10(6) years ago. Two distinctive clones, showing an 85% predicted amino acid sequence identity with each other and 69 to 72% identity with human and mouse LMP-7, were identified from a liver cDNA library of outbred frogs and named XeLMP-7A and XeLMP-7B. XeLMP-7A- and XeLMP-7B-specific probes were used to detect the corresponding genes by using partially inbred frogs with known MHC haplotypes. DNA of the g and j haplotypes hybridized with the XeLMP-7A probe, whereas the f and r haplotype DNA hybridized with the XeLMP-7B probe. These hybridization patterns cosegregated with the MHC haplotypes among offspring of an f/f x f/g cross, and one recombinant revealed that the LMP-7 gene is linked more closely to class II than to class I or class III genes. Taken together, the data indicate that XeLMP-7A and XeLMP-7B are highly diverse alleles at a single locus in the frog MHC. The great allelic diversity can be explained either by coselection with particular class I alleles or by differential silencing of MHC genes in the polyploid X. laevis.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
AIM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/LMP7 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Aug
|
| pubmed:issn |
0022-1767
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
15
|
| pubmed:volume |
155
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1964-71
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:7636247-Alleles,
pubmed-meshheading:7636247-Amino Acid Sequence,
pubmed-meshheading:7636247-Animals,
pubmed-meshheading:7636247-Base Sequence,
pubmed-meshheading:7636247-Blotting, Northern,
pubmed-meshheading:7636247-Blotting, Southern,
pubmed-meshheading:7636247-Cysteine Endopeptidases,
pubmed-meshheading:7636247-DNA, Complementary,
pubmed-meshheading:7636247-Genetic Linkage,
pubmed-meshheading:7636247-Humans,
pubmed-meshheading:7636247-Major Histocompatibility Complex,
pubmed-meshheading:7636247-Mice,
pubmed-meshheading:7636247-Molecular Sequence Data,
pubmed-meshheading:7636247-Multienzyme Complexes,
pubmed-meshheading:7636247-Polymerase Chain Reaction,
pubmed-meshheading:7636247-Proteasome Endopeptidase Complex,
pubmed-meshheading:7636247-Proteins,
pubmed-meshheading:7636247-Xenopus laevis
|
| pubmed:year |
1995
|
| pubmed:articleTitle |
Isolation of Xenopus LMP-7 homologues. Striking allelic diversity and linkage to MHC.
|
| pubmed:affiliation |
Department of Biochemistry, Nagoya City University Medical School, Japan.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|