Fine organization of Bombyx mori fibroin heavy chain gene.

The complete sequence of the Bombyx mori fibroin gene has been determined by means of combining a shotgun sequencing strategy with physical map-based sequencing procedures. It consists of two exons (67 and 15 750 bp, respectively) and one intron (971 bp). The fibroin coding sequence presents a spectacular organization, with a highly repetitive and G-rich (approximately 45%) core flanked by non-repetitive 5' and 3' ends. This repetitive core is composed of alternate arrays of 12 repetitive and 11 amorphous domains. The sequences of the amorphous domains are evolutionarily conserved and the repetitive domains differ from each other in length by a variety of tandem repeats of subdomains of approximately 208 bp which are reminiscent of the repetitive nucleosome organization. A typical composition of a subdomain is a cluster of repetitive units, Ua, followed by a cluster of units, Ub, (with a Ua:Ub ratio of 2:1) flanked by conserved boundary elements at the 3' end. Moreover some repeats are also perfectly conserved at the peptide level indicating that the evolutionary pressure is not identical along the sequence. A tentative model for the constitution and evolution of this unusual gene is discussed.

[1]  C. Earland,et al.  A study of the cystine residues in Bombyx mori and other silks. , 2009, International journal of peptide and protein research.

[2]  Z. Zaidi,et al.  Cystine in silk fibroin, Bombyx mori. , 2009, International journal of protein research.

[3]  K Tanaka,et al.  Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori. , 1999, Biochimica et biophysica acta.

[4]  N. Shimizu,et al.  Construction and characterization of bacterial artificial chromosome libraries from the silkworm, Bombyx mori , 1999, Molecular and General Genetics MGG.

[5]  K. Mita,et al.  A Major Non-LTR Retrotransposon of Bombyx mori, L1Bm , 1997, Journal of Molecular Evolution.

[6]  Y. Suzuki,et al.  Transcriptional regulatory elements in the upstream and intron of the fibroin gene bind three specific factors POU-M1, Bm Fkh and FMBP-1. , 1997, The Biochemical journal.

[7]  K. Tanaka,et al.  Immunological identification of the major disulfide-linked light component of silk fibroin. , 1993, Journal of biochemistry.

[8]  K. Yamaguchi,et al.  Structure of the Bombyx mori fibroin light-chain-encoding gene: upstream sequence elements common to the light and heavy chain. , 1992, Gene.

[9]  K. Matsuno,et al.  Fibroin gene promoter contains a cluster of homeodomain binding sites that interact with three silk gland factors. , 1990, Journal of molecular biology.

[10]  Y. Suzuki,et al.  Homeodomain binding sites in the 5' flanking region of the Bombyx mori silk fibroin light-chain gene. , 1990, Journal of molecular biology.

[11]  F. Corpet Multiple sequence alignment with hierarchical clustering. , 1988, Nucleic acids research.

[12]  K. Mita,et al.  Specific codon usage pattern and its implications on the secondary structure of silk fibroin mRNA. , 1988, Journal of molecular biology.

[13]  Y. Kikuchi,et al.  Further evidence for importance of the subunit combination of silk fibroin in its efficient secretion from the posterior silk gland cells , 1987, The Journal of cell biology.

[14]  H. Ueda,et al.  Tissue-specific and periodic changes in the nuclease sensitivity of the fibroin gene chromatin in the silkworm Bombyx mori. , 1987, Journal of Biological Chemistry.

[15]  P. Couble,et al.  Structural organization of the P25 gene of Bombyx mori and comparative analysis of its 5' flanking DNA with that of the fibroin gene. , 1985, Nucleic acids research.

[16]  Yoshiaki Suzuki,et al.  Faithful transcription initiation of fibroin gene in a homologous cell-free system reveals an enhancing effect of 5′ flanking sequence far upstream , 1981, Cell.

[17]  R. F. Manning,et al.  Internal structure of the silk fibroin gene of Bombyx mori. II. Remarkable polymorphism of the organization of crystalline and amorphous coding sequences. , 1980, The Journal of biological chemistry.

[18]  R. F. Manning,et al.  Internal structure of the silk fibroin gene of Bombyx mori. I The fibroin gene consists of a homogeneous alternating array of repetitious crystalline and amorphous coding sequences. , 1980, The Journal of biological chemistry.

[19]  Y. Tsujimoto,et al.  The dna sequence of bombyx mori fibroin gene including the 5′ flanking, mRNA coding, entire intervening and fibroin protein coding regions , 1979, Cell.

[20]  T. Sasaki,et al.  Studies on silk fibroin of Bombyx mori directly extracted from the silk gland. III. N-terminal analysis and degradation in slightly alkaline solution. , 1974, Journal of biochemistry.

[21]  Y. Suzuki,et al.  Isolation and identification of the messenger RNA for silk fibroin from Bombyx mori. , 1972, Journal of molecular biology.

[22]  R. Fraser,et al.  X-ray diffraction patterns of alpha-fibrous proteins. , 1965, Journal of molecular biology.

[23]  H. Heslot Artificial fibrous proteins: a review. , 1998, Biochimie.

[24]  Jérôme Gouzy,et al.  The ProDom database of protein domain families , 1998, Nucleic Acids Res..

[25]  M. Zama Translational pauses during the synthesis of proteins and mRNA structure. , 1997, Nucleic acids symposium series.

[26]  Shimura Kensuke,et al.  Sequence polymorphisms around the 5'-end of the silkworm fibroin H-chain gene suggesting the occurrence of crossing-over between heteromorphic alleles. , 1985 .

[27]  F LUCAS,et al.  The silk fibroins. , 1958, Advances in protein chemistry.