Literature DB >> 6782490

Differential usage of iso-accepting tRNASer species in silk glands of Bombyx mori.

D Hentzen, A Chevallier, J P Garel.   

Abstract

The rapid development of the silk glands of Bombyx mori during the last larval instar shows two phases. During the first 4 days, in both the middle and posterior parts of the silk glands, the ribosomal machinery is assembled and the synthesis of housekeeping proteins starts. During the second phase (the last 4 days), the middle part of the gland synthesis approximately 45 mg of the silk protein sericin (31% serine) and the posterior part of the gland synthesizes approximately 130 mg of the silk protein fibroin (46% glycine, 29% alanine and 12% serine). Silk fibroin and sericin are detectable by the second day and represent 80 and 50% respectively of the total proteins produced at day 8 (refs 1--4). It is known that the tRNA population of the posterior part of the gland is quantitatively adapted to fibroin codon frequency during this period but little is known about the situation in the middle part except for the observation that it contains more tRNASer than does the posterior part. We show here that the two parts contain, and presumably use, different iso-accepting species of tRNASer, the middle part using tRNASer1, which recognizes AGU and AGC codons, and the posterior part using tRNASer2 which recognizes UCA. We also suggest that this differential adaptation of the tRNASer species is under transcriptional control as the two species are accumulated at different rates, but degraded at the same rate.

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Year:  1981        PMID: 6782490     DOI: 10.1038/290267a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  8 in total

1.  Isolation and sequence analysis of a nuclear tRNA(met-i) gene from soybean.

Authors:  J M Palmer; W R Folk
Journal:  Plant Mol Biol       Date:  1987-01       Impact factor: 4.076

2.  Genes, variant genes, and pseudogenes of the human tRNA(Val) gene family are differentially expressed in HeLa cells and in human placenta.

Authors:  C Schmutzler; H J Gross
Journal:  Nucleic Acids Res       Date:  1990-09-11       Impact factor: 16.971

Review 3.  Protein folding and tRNA biology.

Authors:  Mónica Marín; Tamara Fernández-Calero; Ricardo Ehrlich
Journal:  Biophys Rev       Date:  2017-09-24

4.  Highly repetitive structure and its organization of the silk fibroin gene.

Authors:  K Mita; S Ichimura; T C James
Journal:  J Mol Evol       Date:  1994-06       Impact factor: 2.395

5.  Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis.

Authors:  G P O'Neill; D Söll
Journal:  J Bacteriol       Date:  1990-11       Impact factor: 3.490

6.  tRNA cleavage is a conserved response to oxidative stress in eukaryotes.

Authors:  Debrah M Thompson; Cheng Lu; Pamela J Green; Roy Parker
Journal:  RNA       Date:  2008-08-21       Impact factor: 4.942

7.  Different sequence signatures in the upstream regions of plant and animal tRNA genes shape distinct modes of regulation.

Authors:  Gong Zhang; Radoslaw Lukoszek; Bernd Mueller-Roeber; Zoya Ignatova
Journal:  Nucleic Acids Res       Date:  2010-12-07       Impact factor: 16.971

Review 8.  Silent Polymorphisms: Can the tRNA Population Explain Changes in Protein Properties?

Authors:  Tamara Fernández-Calero; Florencia Cabrera-Cabrera; Ricardo Ehrlich; Mónica Marín
Journal:  Life (Basel)       Date:  2016-02-17
  8 in total

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