The triple-helical domain of alpha 2(VI) collagen is encoded by 19 short exons that are multiples of 9 base pairs.
We have analyzed the structure of the gene coding for the alpha 2(VI) subunit of chicken type VI collagen. The triple-helical domain of this polypeptide is encoded by 19 short exons distributed over 10 kilobase pairs of genomic DNA. These exons begin with the codon for glycine and end with the codon for the Y amino acid of the collagenous triplet Gly-X-Y. The sizes of the exons are integral multiples of 9 base pairs (bp) (27, 36, 45, 54, 63, and 90 bp), the predominant one being 63 bp. The organization of this type VI collagen gene is therefore quite different from that of the fibrillar collagen genes which have evolved by duplication of a primordial 54-bp unit. It also differs from that of the basement membrane collagen genes whose exon/intron boundaries often split the codons for amino acids.
Hayman
A R
AR
Laboratorium für Biochemie I, Eidgenossische Technische Hochschule, Zürich, Switzerland.
Köppel
J
J
Winterhalter
K H
KH
Trueb
B
B
D000595:Amino Acid Sequence; D000818:Animals; D001482:Base Composition; D001483:Base Sequence; D002645:Chickens; D003001:Cloning, Molecular; D003094:Collagen / Q000235:genetics*; D004247:DNA / Q000235:genetics; D015342:DNA Probes; D005091:Exons; D015723:Gene Library; D005796:Genes; D007438:Introns; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011487:Protein Conformation
D015342:DNA Probes; D046911:Macromolecular Substances; D003094:Collagen; D004247:DNA