Literature DB >> 8132637

Post-transcriptional regulation of glutamyl-prolyl-tRNA synthetase in rat salivary gland.

S M Ting1, J D Dignam.   

Abstract

Treatment of rats with isoproterenol resulted in elevated levels of prolyl- and glutamyl-tRNA synthetase activities in the parotid and submandibular glands. This increase in enzyme activity was accompanied by an increase in the bi-functional glutamyl-prolyl-tRNA synthetase and of a low molecular weight form of prolyl-tRNA synthetase. Isoproterenol also induced the synthesis of proline-rich glycoproteins in the parotid and submandibular glands. Withdrawal from the drug was accompanied by a decline in prolyl- and glutamyl-tRNA synthetase activities and by a decline in the levels of proline-rich glycoproteins in the salivary gland. During the time course of isoproterenol treatment, little change in the levels of mRNA encoding the bi-functional glutamyl-prolyl-tRNA synthetase was detected by Northern blot analysis. These results indicate that the synthesis of glutamyl-prolyl-tRNA synthetase is regulated at a post-transcriptional step and that the synthesis of this bifunctional protein may be linked to the utilization of proline and glutamic acid in protein synthesis.

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Year:  1994        PMID: 8132637

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  2 in total

1.  Cloning, sequencing and bacterial expression of human glycine tRNA synthetase.

Authors:  J Williams; S Osvath; T F Khong; M Pearse; D Power
Journal:  Nucleic Acids Res       Date:  1995-04-25       Impact factor: 16.971

2.  Metabolic origin of the fused aminoacyl-tRNA synthetase, glutamyl-prolyl-tRNA synthetase.

Authors:  Sandeep M Eswarappa; Alka A Potdar; Sarthak Sahoo; Santhosh Sankar; Paul L Fox
Journal:  J Biol Chem       Date:  2018-10-11       Impact factor: 5.157

  2 in total

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