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PMID: 6272119 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Structure of the pro alpha 2 (I) collagen gene.

Nature ·Vol. 294 ·No. 5837 ·1981-11-12 ·Pages 129-35

Wozney J, Hanahan D, Tate V, Boedtker H, Doty P

Abstract

Fifty-four kilobase pairs (kbp) of cloned chicken DNA containing the entire 38-kbp pro alpha 2 (I) collagen gene have been isolated and characterized. DNA sequence analysis of a select 4 kbp of the gene has precisely described 14 exons which comprise one-third of the sequences encoding the triple-helical domain of the collagen protein. These exons range in size from 45 to 108 base pairs (bp), are all multiples of the 9 bp that code for the repeating triplet, Gly-X-Y, and have an average size of 70 bp. About 50 introns interrupt this gene. Nevertheless, introns do not separate the coding sequences for the ends of the central triple-helical structural domain and the ends of the propeptide domains.

MeSH Terms
Amino Acid Sequence Animals Base Composition Base Sequence Chickens Cloning, Molecular DNA Restriction Enzymes DNA, Recombinant Genes Nucleic Acid Conformation Nucleic Acid Hybridization Procollagen/genetics
Chemicals
DNA, Recombinant Procollagen DNA Restriction Enzymes
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wozney J
Hanahan D
Tate V
Boedtker H
Doty P
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1981-11-12
Pages
129-35
Language
English
Region
England
NLM ID
0410462
Subset
IM
Databases
GENBANK
J00815, J00825, J00826, J00829, J00830
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