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. 1989 Jun 1;260(2):509–516. doi: 10.1042/bj2600509

Structure of cDNA clones coding for the entire prepro alpha 1 (III) chain of human type III procollagen. Differences in protein structure from type I procollagen and conservation of codon preferences.

L Ala-Kokko 1, S Kontusaari 1, C T Baldwin 1, H Kuivaniemi 1, D J Prockop 1
PMCID: PMC1138697  PMID: 2764886

Abstract

Two overlapping cDNA clones that cover the complete length of the mRNA for human type III procollagen were characterized. The data provided about 2500 base pairs of sequence not previously defined for human type III procollagen. Two tripeptide sequences of -Gly-Xaa-Yaa- were identified that were not detected previously by amino acid sequencing of human type III collagen. The two additional tripeptide units, together with three previously detected, establish that the alpha 1 (III) chain is 15 amino acids longer than either the alpha 1 (I) or alpha 2 (I) chains of type I collagen. The additional tripeptide units made hydropathy plots of the N-terminal and C-terminal regions of type III collagen distinctly different from those of type I collagen. The data also demonstrated that human type III procollagen has the same third base preference in codons for glycine, proline and alanine that was previously found with human and chick type I procollagen. In addition, comparison of two cDNA clones from the same individual revealed a variation in structure in that the codon for amino acid 880 of the alpha 1 (III) chain was -CTT- for leucine in one clone and -TTT- for phenylalanine in the other.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Baldwin C. T., Constantinou C. D., Dumars K. W., Prockop D. J. A single base mutation that converts glycine 907 of the alpha 2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix. J Biol Chem. 1989 Feb 15;264(5):3002–3006. [PubMed] [Google Scholar]
  2. Bernard M. P., Chu M. L., Myers J. C., Ramirez F., Eikenberry E. F., Prockop D. J. Nucleotide sequences of complementary deoxyribonucleic acids for the pro alpha 1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution. Biochemistry. 1983 Oct 25;22(22):5213–5223. doi: 10.1021/bi00291a023. [DOI] [PubMed] [Google Scholar]
  3. Bernard M. P., Myers J. C., Chu M. L., Ramirez F., Eikenberry E. F., Prockop D. J. Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies structurally conserved features of the protein and the gene. Biochemistry. 1983 Mar 1;22(5):1139–1145. doi: 10.1021/bi00274a023. [DOI] [PubMed] [Google Scholar]
  4. Boedtker H., Finer M., Aho S. The structure of the chicken alpha 2 collagen gene. Ann N Y Acad Sci. 1985;460:85–116. doi: 10.1111/j.1749-6632.1985.tb51159.x. [DOI] [PubMed] [Google Scholar]
  5. Brandt A., Glanville R. W., Hörlein D., Bruckner P., Timpl R., Fietzek P. P., Kühn K. Complete amino acid sequence of the N-terminal extension of calf skin type III procollagen. Biochem J. 1984 Apr 15;219(2):625–634. doi: 10.1042/bj2190625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Chu M. L., Weil D., de Wet W., Bernard M., Sippola M., Ramirez F. Isolation of cDNA and genomic clones encoding human pro-alpha 1 (III) collagen. Partial characterization of the 3' end region of the gene. J Biol Chem. 1985 Apr 10;260(7):4357–4363. [PubMed] [Google Scholar]
  7. Fietzek P. P., Allmann H., Rauterberg J., Henkel W., Wachter E., Kühn K. The covalent structure of calf skin type III collagen. I. The amino acid sequence of the amino terminal region of the alpha 1(III) chain (position 1--222). Hoppe Seylers Z Physiol Chem. 1979 Jul;360(7):809–820. doi: 10.1515/bchm2.1979.360.2.809. [DOI] [PubMed] [Google Scholar]
  8. Fleischmajer R., Timpl R., Tuderman L., Raisher L., Wiestner M., Perlish J. S., Graves P. N. Ultrastructural identification of extension aminopropeptides of type I and III collagens in human skin. Proc Natl Acad Sci U S A. 1981 Dec;78(12):7360–7364. doi: 10.1073/pnas.78.12.7360. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Glanville R. W., Fietzek P. P. Amino acid sequence to the N-terminal non-triple helical cross link region of type III collagen. FEBS Lett. 1976 Nov 15;72(1):99–102. doi: 10.1016/0014-5793(76)80907-6. [DOI] [PubMed] [Google Scholar]
  10. Gubler U., Hoffman B. J. A simple and very efficient method for generating cDNA libraries. Gene. 1983 Nov;25(2-3):263–269. doi: 10.1016/0378-1119(83)90230-5. [DOI] [PubMed] [Google Scholar]
  11. Kuivaniemi H., Tromp G., Chu M. L., Prockop D. J. Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation. Biochem J. 1988 Jun 15;252(3):633–640. doi: 10.1042/bj2520633. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Liau G., Mudryj M., de Crombrugghe B. Identification of the promoter and first exon of the mouse alpha 1 (III) collagen gene. J Biol Chem. 1985 Mar 25;260(6):3773–3777. [PubMed] [Google Scholar]
  13. Loidl H. R., Brinker J. M., May M., Pihlajaniemi T., Morrow S., Rosenbloom J., Myers J. C. Molecular cloning and carboxyl-propeptide analysis of human type III procollagen. Nucleic Acids Res. 1984 Dec 21;12(24):9383–9394. doi: 10.1093/nar/12.24.9383. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mankoo B. S., Dalgleish R. Human pro alpha 1(III) collagen: cDNA sequence for the 3' end. Nucleic Acids Res. 1988 Mar 25;16(5):2337–2337. doi: 10.1093/nar/16.5.2337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Messing J. New M13 vectors for cloning. Methods Enzymol. 1983;101:20–78. doi: 10.1016/0076-6879(83)01005-8. [DOI] [PubMed] [Google Scholar]
  16. Miskulin M., Dalgleish R., Kluve-Beckerman B., Rennard S. I., Tolstoshev P., Brantly M., Crystal R. G. Human type III collagen gene expression is coordinately modulated with the type I collagen genes during fibroblast growth. Biochemistry. 1986 Mar 25;25(6):1408–1413. doi: 10.1021/bi00354a033. [DOI] [PubMed] [Google Scholar]
  17. Prockop D. J., Kivirikko K. I. Heritable diseases of collagen. N Engl J Med. 1984 Aug 9;311(6):376–386. doi: 10.1056/NEJM198408093110606. [DOI] [PubMed] [Google Scholar]
  18. Sanger F., Nicklen S., Coulson A. R. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5463–5467. doi: 10.1073/pnas.74.12.5463. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Seyer J. M., Kang A. H. Covalent structure of collagen: amino acid sequence of alpha 1(III)-CB9 from type III collagen of human liver. Biochemistry. 1981 Apr 28;20(9):2621–2627. doi: 10.1021/bi00512a040. [DOI] [PubMed] [Google Scholar]
  20. Seyer J. M., Mainardi C., Kang A. H. Covalent structure of collagen: amino acid sequence of alpha 1 (III)-CB5 from type III collagen of human liver. Biochemistry. 1980 Apr 15;19(8):1583–1589. doi: 10.1021/bi00549a008. [DOI] [PubMed] [Google Scholar]
  21. Toman P. D., Ricca G. A., de Crombrugghe B. Nucleotide sequence of a cDNA coding for the amino-terminal region of human prepro alpha 1(III) collagen. Nucleic Acids Res. 1988 Jul 25;16(14B):7201–7201. doi: 10.1093/nar/16.14.7201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tromp G., Kuivaniemi H., Stacey A., Shikata H., Baldwin C. T., Jaenisch R., Prockop D. J. Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen. Biochem J. 1988 Aug 1;253(3):919–922. doi: 10.1042/bj2530919. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Wood L., Theriault N., Vogeli G. Complete nucleotide sequence of the N-terminal domains of the murine alpha-1 type-III collagen chain. Gene. 1987;61(2):225–230. doi: 10.1016/0378-1119(87)90117-x. [DOI] [PubMed] [Google Scholar]
  24. Yamada Y., Kühn K., de Crombrugghe B. A conserved nucleotide sequence, coding for a segment of the C-propeptide, is found at the same location in different collagen genes. Nucleic Acids Res. 1983 May 11;11(9):2733–2744. doi: 10.1093/nar/11.9.2733. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Yamada Y., Liau G., Mudryj M., Obici S., de Crombrugghe B. Conservation of the sizes for one but not another class of exons in two chick collagen genes. 1984 Jul 26-Aug 1Nature. 310(5975):333–337. doi: 10.1038/310333a0. [DOI] [PubMed] [Google Scholar]
  26. Yamada Y., Mudryj M., Sullivan M., de Crombrugghe B. Isolation and characterization of a genomic clone encoding chick alpha 1 type III collagen. J Biol Chem. 1983 Mar 10;258(5):2758–2761. [PubMed] [Google Scholar]
  27. Yamada Y., Mudryj M., de Crombrugghe B. A uniquely conserved regulatory signal is found around the translation initiation site in three different collagen genes. J Biol Chem. 1983 Dec 25;258(24):14914–14919. [PubMed] [Google Scholar]

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