Specifie codon usage pattern and its implications on the secondary structure of silk fibroin mRNA

Mita, Kazuei; Ichimura, Sachiko; Zama, Mitsuo; James, Tharappel C.

doi:10.1016/0022-2836(88)90117-9

Cited by 92 publications

(60 citation statements)

References 33 publications

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“…The literature contains other interesting examples of modulation of translation by discontinuities in the rate of ribosome progression mediated apparently by conformational constraints in the mRNA (34)(35)(36)(37)(38).…”

Section: Discussionmentioning

confidence: 99%

Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes.

Kozak¹

1990

Proc. Natl. Acad. Sci. U.S.A.

507

405

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Section: Discussionmentioning

confidence: 99%

Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes.

Kozak¹

1990

Proc. Natl. Acad. Sci. U.S.A.

507

405

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“…However, all repeats within the rib gene, and also within the ␣ gene, are apparently identical. A possible alternative explanation for the identity of the repeats could be the existence of base pairing within RNA secondary structures, which might limit mutation frequencies (25). However, it is clear that mutations can accumulate in the repeat region, because the repeats of Rib and ␣ must have evolved from a common predecessor (Fig.…”

Section: Discussionmentioning

confidence: 99%

Identification of a Family of Streptococcal Surface Proteins with Extremely Repetitive Structure

Wästfelt

Stålhammar‐Carlemalm

Delisse³

et al. 1996

Journal of Biological Chemistry

119

158

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The group B Streptococcus (GBS) causes the majority of life-threatening bacterial infections in newborn children. Most GBS strains isolated from such infections express a surface protein, designated Rib, that confers protective immunity and therefore is of interest for analysis of pathogenetic mechanisms. Sequence analysis demonstrated that Rib has an exceptionally long signal peptide (55 amino acid residues) and 12 repeats (79 amino acid residues each) that account for >80% of the sequence of the mature protein. The repeats are identical even at the DNA level, indicating that an efficient mechanism operates to maintain a highly repetitive structure in Rib. The structure of Rib is similar to that of ␣, a previously characterized surface protein that is common among GBS strains lacking Rib. However, highly purified preparations of Rib and ␣ did not crossreact immunologically, although the two proteins show extensive amino acid residue identity (47% in the repeat region). When analyzed in Western blots, Rib and ␣ give rise to a regularly spaced ladder pattern, apparently due to hydrolysis of acid-labile Asp-Pro bonds in the repeats. We conclude that Rib and ␣ are members of a novel family of streptococcal surface proteins with unusual repetitive structure.

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“…Both MaSp1 and MaSp2 show a similar codon usage with a preference for A or T as the third nucleotide. This is likely to reduce the high degree of secondary structure of the transcript (Mita et al, 1988;Hinman and Lewis, 1992). (At least this has been observed in the silkworm where stretches of G and C are thought to create recombination hotspots, something which could destabilise the genes [Mita et al, 1994].)…”

Section: The Silk; Genes and Primary Structure Of The Proteinsmentioning

confidence: 99%

Spider Silk Proteins – Mechanical Property and Gene Sequence

et al. 2005

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-Spiders spin up to seven different types of silk and each type possesses different mechanical properties. The reports on base sequences of spider silk protein genes have gained importance as the mechanical properties of silk fibers have been revealed. This review aims to link recent molecular data, often translated into amino acid sequences and predicted three dimensional structural motifs, to known mechanical properties.

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Specifie codon usage pattern and its implications on the secondary structure of silk fibroin mRNA

Cited by 92 publications

References 33 publications

Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes.

Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes.

Identification of a Family of Streptococcal Surface Proteins with Extremely Repetitive Structure

Spider Silk Proteins – Mechanical Property and Gene Sequence

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