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Author Žurovec, M. ♦ Kodrík, D. ♦ Yang, C. ♦ Sehnal, F. ♦ Scheller, K.
Source SpringerLink
Content type Text
Publisher Springer-Verlag
File Format PDF
Copyright Year ©1998
Language English
Subject Domain (in DDC) Social sciences ♦ Sociology & anthropology
Abstract The water-insoluble core of lepidopteran silk is composed of four major proteins, but only three genes have been identified. This study demonstrates that the 29- and 30-kDa components of Galleria mellonella silk are derived from a single gene designated P25. The gene is expressed exclusively in the posterior section of the silk glands as a 2-kb mRNA, which accumulates in the feeding larvae and declines at molting. The mRNA encodes a peptide of 24 864 Da that exhibits 51% identity with the putative product of the P25 gene of Bombyx. The conservation of several amino acid stretches, including the relative positions of all 8 cysteines in the mature polypeptide, implies that the P25 proteins play similar, and apparently significant roles in silk formation in the two species. A Galleria P25 cDNA yields a peptide of about 25 kDa when translated in vitro; the 29- and 30-kDa forms present in the silk are derived from this primary translation product by differential glycosylation.
ISSN 00268925
Age Range 18 to 22 years ♦ above 22 year
Educational Use Research
Education Level UG and PG
Learning Resource Type Article
Publisher Date 1998-02-19
Publisher Place Berlin/Heidelberg
e-ISSN 14321874
Journal Molecular and General Genetics MGG
Volume Number 257
Issue Number 3
Page Count 7
Starting Page 264
Ending Page 270


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Source: SpringerLink