Molecular cloning and characterization of lustrin A, a matrix protein from shell and pearl nacre of Haliotis rufescens

被引:313
作者
Shen, XY
Belcher, AM
Hansma, PK
Stucky, GD
Morse, DE [1 ]
机构
[1] Univ Calif Santa Barbara, Dept Mol Cellular & Dev Biol, Santa Barbara, CA 93106 USA
[2] Univ Calif Santa Barbara, Dept Phys, Santa Barbara, CA 93106 USA
[3] Univ Calif Santa Barbara, Dept Chem, Santa Barbara, CA 93106 USA
[4] Univ Calif Santa Barbara, Dept Mat, Santa Barbara, CA 93106 USA
[5] Univ Calif Santa Barbara, Ctr Marine Biotechnol, Santa Barbara, CA 93106 USA
[6] Univ Calif Santa Barbara, Mat Res Lab, Santa Barbara, CA 93106 USA
关键词
D O I
10.1074/jbc.272.51.32472
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A specialized extracellular matrix of proteins and polysaccharides controls the morphology and packing of calcium carbonate crystals and becomes occluded within the mineralized composite during formation of the molluscan shell and pearl. We have cloned and characterized the cDNA coding for Lustrin A, a newly described matrix protein from the nacreous layer of the shell and pearl produced by the abalone, Haliotis rufescens, a marine gastropod mollusc. The full-length cDNA is 4,439 base pairs (bp) long and contains an open reading frame coding for 1,428 amino acids. The deduced amino acid sequence reveals a highly modular structure with a high proportion of Ser (16%), Pro (14%), Gly (13%), and Cys (9%). The protein contains ten highly conserved cysteine-rich domains interspersed by eight proline-rich domains; a glycine-and serine-rich domain lies between the two cysteine-rich domains nearest the C terminus, and these are followed by a basic domain and a C-terminal domain that is highly similar to known protease inhibitors. The glycine-and serine-rich domain and at least one of the proline-rich domains show sequence similarity to proteins of two extracellular matrix superfamilies (one of which also is involved in the mineralized matrixes of bone, dentin, and avian eggshell). The arrangement of alternating cysteine-rich domains and proline-rich domains is strikingly similar to that found in frustulins, the proteins that are integral to the silicified cell wall of diatoms. Its modular structure suggests that Lustrin A is a multifunctional protein, whereas the occurrence of related sequences suggest it is a member of a multiprotein family.
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页码:32472 / 32481
页数:10
相关论文
共 83 条
  • [1] [Anonymous], 1983, Biomineralization and Biological Metal Accumulation
  • [2] BIOMINERALIZATION AND EGGSHELLS - CELL-MEDIATED ACELLULAR COMPARTMENTS OF MINERALIZED EXTRACELLULAR-MATRIX
    ARIAS, JL
    FINK, DJ
    XIAO, SQ
    HEUER, AH
    CAPLAN, AI
    [J]. INTERNATIONAL REVIEW OF CYTOLOGY - A SURVEY OF CELL BIOLOGY, VOL 145, 1993, 145 : 217 - 250
  • [3] BEG OU, 1986, EUR J BIOCHEM, V159, P195, DOI 10.1111/j.1432-1033.1986.tb09852.x
  • [4] Control of crystal phase switching and orientation by soluble mollusc-shell proteins
    Belcher, AM
    Wu, XH
    Christensen, RJ
    Hansma, PK
    Stucky, GD
    Morse, DE
    [J]. NATURE, 1996, 381 (6577) : 56 - 58
  • [5] BELCHER AM, 1996, THESIS U CALIFORNIA
  • [6] BELCHER AM, 1997, IN PRESS ACTA METAL
  • [7] AN ELECTRON MICROSCOPE STUDY OF FORMATION OF NACREOUS LAYER IN SHELL OF CERTAIN BIVALVE MOLLUSCS
    BEVELANDER, G
    NAKAHARA, H
    [J]. CALCIFIED TISSUE RESEARCH, 1969, 3 (01): : 84 - +
  • [8] Conchiolin-protein in aragonite shells of mollusks
    Bowen, CE
    Tang, H
    [J]. COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY A-PHYSIOLOGY, 1996, 115 (04): : 269 - 275
  • [9] BRUNET PCJ, 1967, ENDEAVOUR, V26, P68
  • [10] AROMATIC-AROMATIC INTERACTION - A MECHANISM OF PROTEIN-STRUCTURE STABILIZATION
    BURLEY, SK
    PETSKO, GA
    [J]. SCIENCE, 1985, 229 (4708) : 23 - 28