Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
34
|
pubmed:dateCreated |
1989-1-3
|
pubmed:databankReference | |
pubmed:abstractText |
Type X collagen, expressed by hypertrophic chondrocytes, consists of homotrimeric molecules with subunits that are only about one-half the size of the polypeptides of fibrillar collagens. In this report we describe for the first time the complete primary structure of type X collagen, based on cloning and sequencing of cDNA and genomic DNA. A comparison between the nucleotide sequences of the cDNA and genomic DNA clones has also allowed determination of the complete exon structure of the type X collagen gene. Our results demonstrate that the primary translation product of the chicken type X collagen mRNA is 682 amino acid residues long with a calculated molecular mass of 67,317 Da for the nonhydroxylated form. This calculated molecular mass is in excellent agreement with the observed electrophoretic mobility of cell-free translation products with both poly(A)+ RNA isolated from chondrocytes as well as RNA transcribed in vitro from a full length cDNA construct. It is also in agreement with the observed size of type X collagen polypeptides isolated from the media of cultured hypertrophic chondrocytes. Thus, our data exclude the possibility of a high molecular weight precursor form of type X collagen. Our results also confirm that the chicken type X gene has a most unusual exon structure when compared to other vertebrate collagen genes. The gene has only three exons. One exon (97 base pairs (bp)), codes for most of the 5'-untranslated region of the mRNA, a second exon (159 bp) codes for the signal peptide and a short non-triple-helical domain, while the third exon (2136 bp) contains the coding region for the entire triple-helix and a large non-triple-helical carboxyl domain.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
263
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
18378-85
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:2461368-Amino Acid Sequence,
pubmed-meshheading:2461368-Animals,
pubmed-meshheading:2461368-Base Sequence,
pubmed-meshheading:2461368-Chick Embryo,
pubmed-meshheading:2461368-Cloning, Molecular,
pubmed-meshheading:2461368-Collagen,
pubmed-meshheading:2461368-DNA,
pubmed-meshheading:2461368-Exons,
pubmed-meshheading:2461368-Genes,
pubmed-meshheading:2461368-Growth Plate,
pubmed-meshheading:2461368-Introns,
pubmed-meshheading:2461368-Molecular Sequence Data,
pubmed-meshheading:2461368-Protein Biosynthesis,
pubmed-meshheading:2461368-RNA,
pubmed-meshheading:2461368-Transcription, Genetic
|
pubmed:year |
1988
|
pubmed:articleTitle |
The type X collagen gene. Intron sequences split the 5'-untranslated region and separate the coding regions for the non-collagenous amino-terminal and triple-helical domains.
|
pubmed:affiliation |
Department of Anatomy and Cellular Biology, Harvard Medical School, Boston, Massachusetts 02115.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|