Structure of the gene for cartilage matrix protein, a modular protein of the extracellular matrix. Exon/intron organization, unusual splice sites, and relation to α chains of β2 integrins, von Willebrand factor, complement factors B and C2, and epidermal growth factor

I. Kiss, F. Deak, R. G. Holloway, H. Delius, K. A. Mebust, E. Frimberger, W. S. Argraves, P. A. Tsonis, N. Winterbottom, P. F. Goetinck

Research output: Contribution to journalArticle

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Abstract

The entire gene for chicken cartilage matrix protein (CMP) has been isolated and characterized by restriction mapping, electron microscopy, nuclease S1 mapping, and sequence analysis. The gene, which is present in a single copy in the chicken genome, is 18 kilobase pairs long and comprises eight exons and seven introns. It has two transcription initiation sites, 8 base pairs from each other. A sequence very homologous to the consensus nuclear factor III binding-site sequence, a CAT- and a TATA-like sequence are found in the promoter region and ATTAAA is used as a polyadenylation signal. The nucleotide sequence defines a primary translation product of 493 amino acids which consists of a 23-amino acid signal peptide and two large repeated domains connected by an epidermal growth factor module. Amino acid sequences homologous to those of the repeated domains are present in the type A repeats of von Willebrand factor, complement factors B and C2, and in the α chains of the integrins Mac-1, p150,95, and LFA-1. The exon-intron structure indicates that the CMP gene may have arisen by exon duplication and exon shuffling during evolution. The GT-AG splice rule cannot be applied for the excision of the last intron of the CMP pre-mRNA. The donor splice site of intron G is basically different from the consensus sequence indicating that a novel type of splicing mechanism might exist in cartilage.

Original languageEnglish
Pages (from-to)8126-8134
Number of pages9
JournalJournal of Biological Chemistry
Volume264
Issue number14
Publication statusPublished - 1989

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Matrilin Proteins
Complement Factor B
Extracellular Matrix Proteins
von Willebrand Factor
Epidermal Growth Factor
Integrins
Introns
Exons
Genes
Amino Acids
Chickens
Octamer Transcription Factor-1
Amino Acid Sequence Homology
Lymphocyte Function-Associated Antigen-1
Restriction Mapping
RNA Splice Sites
Polyadenylation
Transcription Initiation Site
RNA Precursors
Consensus Sequence

ASJC Scopus subject areas

  • Biochemistry

Cite this

Structure of the gene for cartilage matrix protein, a modular protein of the extracellular matrix. Exon/intron organization, unusual splice sites, and relation to α chains of β2 integrins, von Willebrand factor, complement factors B and C2, and epidermal growth factor. / Kiss, I.; Deak, F.; Holloway, R. G.; Delius, H.; Mebust, K. A.; Frimberger, E.; Argraves, W. S.; Tsonis, P. A.; Winterbottom, N.; Goetinck, P. F.

In: Journal of Biological Chemistry, Vol. 264, No. 14, 1989, p. 8126-8134.

Research output: Contribution to journalArticle

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abstract = "The entire gene for chicken cartilage matrix protein (CMP) has been isolated and characterized by restriction mapping, electron microscopy, nuclease S1 mapping, and sequence analysis. The gene, which is present in a single copy in the chicken genome, is 18 kilobase pairs long and comprises eight exons and seven introns. It has two transcription initiation sites, 8 base pairs from each other. A sequence very homologous to the consensus nuclear factor III binding-site sequence, a CAT- and a TATA-like sequence are found in the promoter region and ATTAAA is used as a polyadenylation signal. The nucleotide sequence defines a primary translation product of 493 amino acids which consists of a 23-amino acid signal peptide and two large repeated domains connected by an epidermal growth factor module. Amino acid sequences homologous to those of the repeated domains are present in the type A repeats of von Willebrand factor, complement factors B and C2, and in the α chains of the integrins Mac-1, p150,95, and LFA-1. The exon-intron structure indicates that the CMP gene may have arisen by exon duplication and exon shuffling during evolution. The GT-AG splice rule cannot be applied for the excision of the last intron of the CMP pre-mRNA. The donor splice site of intron G is basically different from the consensus sequence indicating that a novel type of splicing mechanism might exist in cartilage.",
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