Literature DB >> 1977388

The primary structure of rat ribosomal protein L12.

K Suzuki1, J Olvera, I G Wool.   

Abstract

The covalent structure of the rat 60S subunit protein L12 which is a component of the ribosomal elongation factor binding domain was deduced from the sequence of nucleotides in a recombinant cDNA and confirmed from the NH2-terminal amino acid sequence of the protein. L12 has 165 amino acids and a molecular weight of 17,834. Hybridization of the cDNA to digests of nuclear DNA suggests that there are 11-13 copies of the L12 gene. The mRNA for the protein is about 800 nucleotides in length. Rat L12 is homologous to Saccharomyces cerevisiae L15. The cDNA contains the highly repetitive DNA sequence, R.dre.1, in the 3' noncoding region.

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Year:  1990        PMID: 1977388     DOI: 10.1016/s0006-291x(05)80169-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

1.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1991-02-11       Impact factor: 16.971

2.  The primary structure of human ribosomal protein L12.

Authors:  W Chu; D H Presky; R A Swerlick; D K Burns
Journal:  Nucleic Acids Res       Date:  1993-02-11       Impact factor: 16.971

3.  Molecular phylogenies based on ribosomal protein L11, L1, L10, and L12 sequences.

Authors:  D Liao; P P Dennis
Journal:  J Mol Evol       Date:  1994-04       Impact factor: 2.395

Review 4.  Involvement of Dcr1 in post-transcriptional regulation of gene expression in Schizosaccharomyces pombe.

Authors:  Lise-Andree Gobeil; Pierre Plante; Mina Rohani; Marc Ouellette; Patrick Provost
Journal:  Front Biosci       Date:  2008-01-01
  4 in total

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