Fine organization of Bombyx mori fibroin heavy chain gene.
نویسندگان
چکیده
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.
منابع مشابه
The silk proteins, sericin and fibroin in silkworm, Bombyx mori Linn., - a review
The domesticated silkworm, Bombyx mori Linn., a lepidopteran molecular model and an important economic insect that are emerging as an ideal molecular genetic resource for solving a broad range of biological problems. The silkworm, B. mori produces massive amount of silk proteins during the final stage of larval development. These proteins are stored in the middle silk gland and they are dischar...
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ورودعنوان ژورنال:
- Nucleic acids research
دوره 28 12 شماره
صفحات -
تاریخ انتشار 2000