Light-chain fibroin of Galleria mellonella L.
The posterior section of Galleria mellonella silk glands contains two abundant mRNAs that are identical except for the non-coding tail, which includes either two (1.1 kb mRNA) or three (1.2 kb mRNA) consensus sequences for polyadenylation sites. The transcripts are 40% homologous in the coding as well as non-coding regions with the mRNA encoding light-chain fibroin (L-fibroin) in Bombyx mori; the deduced translation product shows 43% identity with the Bombyx L-fibroin peptide, with all three cysteines conserved. Amino acid analysis of the N-termini of Galleria silk proteins revealed that L-fibroin (25 kDa) occurs in two isoforms, the shorter one lacking the Ala-Pro dipeptide residue at its N-terminus. The 29 and 30 kDa Galleria silk proteins appear to be homologs of Bombyx silk component P25. The results suggest that evolutionary diversification of Galleria and Bombyx L-fibroins involves alternative polyadenylation and proteolytic processing sites.
Zurovec
M
M
Entomological Institute, Academy of Sciences, Ceské Budĕjovice, Czech Republic.
Vasková
M
M
Kodrík
D
D
Sehnal
F
F
Kumaran
A K
AK
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D012831:Bombyx / Q000235:genetics; D018076:DNA, Complementary / Q000235:genetics; D005349:Fibroins / Q000737:chemistry* / Q000235:genetics*; D007301:Insect Hormones / Q000737:chemistry / Q000235:genetics*; D007814:Larva; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009036:Moths / Q000235:genetics*; D011061:Poly A / Q000378:metabolism; D011487:Protein Conformation; D011679:Pupa; D012333:RNA, Messenger / Q000378:metabolism; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D012689:Sequence Homology, Nucleic Acid
D018076:DNA, Complementary; D007301:Insect Hormones; D012333:RNA, Messenger; D011061:Poly A; D005349:Fibroins