Translational pauses during the synthesis of proteins and mRNA structure.
Translational pauses are observed during a spider fibroin synthesis (1,2). The spider major ampullate (dragline) silk of the spider Nephila clavipes is composed of multiple proteins. The amino acid sequences of the partial cDNA clones for the two major dragline silk fibroin components (Spidroin 1 and 2) exhibit repetitive motifs (3,4). Our detailed inspection of the nucleotide sequences of the repetitive motifs revealed highly selective site-specific codon usage patterns within a motif, suggesting that the secondary structure of the spider fibroin mRNA is optimized by the nucleotide sequence of the fibroin gene. The results, combined with our preceding results on silk fibroin from Bombyx mori (5) suggest that translational pauses of spider silk are interpreted in terms of the mRNA secondary structure.
Zama
M
M
National Institute of Radiological Sciences, Chiba-shi, Japan.
D000595:Amino Acid Sequence; D000818:Animals; D012831:Bombyx; D003062:Codon / Q000235:genetics; D017124:Conserved Sequence; D005349:Fibroins / Q000096:biosynthesis / Q000737:chemistry; D019476:Insect Proteins; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D011506:Proteins / Q000737:chemistry; D012333:RNA, Messenger / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D047011:Silk; D013112:Spiders / Q000378:metabolism*
D003062:Codon; D019476:Insect Proteins; D011506:Proteins; D012333:RNA, Messenger; D047011:Silk; C086087:spidroin 1; C076815:spidroin 2; D005349:Fibroins