Literature DB >> 6493217

Structural organization of high-Mr mammalian aminoacyl-tRNA synthetases. Comparison of multi-enzyme complexes from different sources.

C V Dang, C V Dang.   

Abstract

Many mammalian aminoacyl-tRNA synthetases have been isolated as high-Mr multi-enzyme complexes. These complexes often contain variable contents of synthetase activities. The complexes may also contain molecules other than synthetases such as tRNA. The observed variations in size, polypeptide composition, and content of enzyme activities of the high-Mr synthetase complexes have been sources of confusion in the understanding of the structural organization of these complexes. A unified scheme of structural organization which encompasses most observations on high-Mr complexes reported in the literature is presented.

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Year:  1984        PMID: 6493217     DOI: 10.1007/bf00285220

Source DB:  PubMed          Journal:  Mol Cell Biochem        ISSN: 0300-8177            Impact factor:   3.396


  32 in total

1.  Isolation and partial characterization of an aminoacyl-tRNA synthetase complex from rabbit reticulocytes.

Authors:  K Som; B Hardesty
Journal:  Arch Biochem Biophys       Date:  1975-02       Impact factor: 4.013

2.  Occurrence of a complex of aminoacryl-tRNA synthetases in lactating rat mammary gland.

Authors:  P Hele; L Hebert
Journal:  Biochim Biophys Acta       Date:  1977-12-02

3.  Processing of tRNA is accomplished by a high-molecular-weight enzyme complex.

Authors:  P F Agris; T Playl; L Goldman; E Horton; D Woolverton; D Setzer; C Rodi
Journal:  Recent Results Cancer Res       Date:  1983

4.  Low molecular weight aspartyl-tRNA synthetase from porcine thyroid. Purification, characterization, and heterogeneity.

Authors:  G J Vellekamp; C L Coyle; F J Kull
Journal:  J Biol Chem       Date:  1983-07-10       Impact factor: 5.157

Review 5.  High molecular weight complexes of eukaryotic aminoacyl-tRNA synthetases.

Authors:  C V Dang; D C Yang
Journal:  Int J Biochem       Date:  1982

6.  Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. III. Assignment of aminoacyl-tRNA synthetase activities to the polypeptide components of the complexes.

Authors:  M Mirande; B Cirakoğlu; J P Waller
Journal:  J Biol Chem       Date:  1982-09-25       Impact factor: 5.157

7.  Stoichiometry and composition of an aminoacyl-tRNA synthetase complex from rat liver.

Authors:  D L Johnson; D C Yang
Journal:  Proc Natl Acad Sci U S A       Date:  1981-07       Impact factor: 11.205

8.  Characterization of a proteolipid complex of aminoacyl-tRNA synthetases and transfer RNA from rat liver.

Authors:  H J Saxholm; H C Pitot
Journal:  Biochim Biophys Acta       Date:  1979-05-24

9.  Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. II. Structural characterization of the polypeptide components and immunological identification of the methionyl-tRNA synthetase subunit.

Authors:  M Mirande; O Kellermann; J P Waller
Journal:  J Biol Chem       Date:  1982-09-25       Impact factor: 5.157

10.  Seven mammalian aminoacyl-tRNA synthetases co-purified as high molecular weight entities are associated within the same complex.

Authors:  M Mirande; Y Gache; D Le Corre; J P Waller
Journal:  EMBO J       Date:  1982       Impact factor: 11.598

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  2 in total

Review 1.  Higher eukaryotic aminoacyl-tRNA synthetases in physiologic and pathologic states.

Authors:  C V Dang; C V Dang
Journal:  Mol Cell Biochem       Date:  1986-08       Impact factor: 3.396

Review 2.  Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic.

Authors:  C V Dang; C V Dang
Journal:  Biochem J       Date:  1986-10-15       Impact factor: 3.857

  2 in total

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