Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (420K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (157)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Zhou, C.-Z.
Right arrow Articles by Li, Z.-G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhou, C.-Z.
Right arrow Articles by Li, Z.-G.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 2000, Vol. 28, No. 12 2413-2419
© 2000 Oxford University Press

Fine organization of Bombyx mori fibroin heavy chain gene

Cong-Zhao Zhou1,2,3, Fabrice Confalonieri1,*, Nadine Medina1, Yvan Zivanovic1, Catherine Esnault1, Tie Yang2,3, Michel Jacquet1, Joel Janin4, Michel Duguet1, Roland Perasso2 and Zhen-Gang Li3

1Institut de Génétique et Microbiologie and 2Laboratoire de Biologie Cellulaire 4, Université Paris-Sud et CNRS, 91405 Orsay Cedex, France, 3Department of Biology, University of Science and Technology of China, Hefei Anhui 230027, People’s Republic of China and 4Laboratoire d’Enzymologie et Biochimie Structurales, CNRS, 91198 Gif-sur-Yvette, France

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 (~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 ~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.

* To whom correspondence should be addressed. Tel: +33 1 69 15 46 20; Fax: +33 1 69 15 72 96; Email: confalonieri@igmors.u-psud.fr


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Genome ResHome page
T. D. Sutherland, P. M. Campbell, S. Weisman, H. E. Trueman, A. Sriskantha, W. J. Wanjura, and V. S. Haritos
A highly divergent gene cluster in honey bees encodes a novel silk family
Genome Res., November 1, 2006; 16(11): 1414 - 1421.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
M. Yang and T. Asakura
Design, Expression and Solid-State NMR Characterization of Silk-Like Materials Constructed from Sequences of Spider Silk, Samia cynthia ricini and Bombyx mori Silk Fibroins
J. Biochem., June 1, 2005; 137(6): 721 - 729.
[Abstract] [Full Text] [PDF]

Home page
 J. Nutr.Home page
C.-K. Hyun, I.-Y. Kim, and S. C. Frost
Soluble Fibroin Enhances Insulin Sensitivity and Glucose Metabolism in 3T3-L1 Adipocytes
J. Nutr., December 1, 2004; 134(12): 3257 - 3263.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. Fedic, M. Zurovec, and F. Sehnal
Correlation between Fibroin Amino Acid Sequence and Physical Silk Properties
J. Biol. Chem., September 12, 2003; 278(37): 35255 - 35264.
[Abstract] [Full Text] [PDF]

Home page
 J BiochemHome page
J. Yao and T. Asakura
Synthesis and Structural Characterization of Silk-Like Materials Incorporated with an Elastic Motif
J. Biochem., January 1, 2003; 133(1): 147 - 154.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Zurovec and F. Sehnal
Unique Molecular Architecture of Silk Fibroin in the Waxmoth, Galleria mellonella
J. Biol. Chem., June 14, 2002; 277(25): 22639 - 22647.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.