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

Chi V. Danga, Chuan V. Dang

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)131-136
Number of pages6
JournalMolecular and Cellular Biochemistry
Volume63
Issue number2
DOIs
StatePublished - Sep 1984
Externally publishedYes

Fingerprint

Amino Acyl-tRNA Synthetases
Ligases
Enzymes
Enzyme activity
Transfer RNA
Peptides
Molecules
Chemical analysis
Multienzyme Complexes

Keywords

  • aminoacyl-tRNA synthetase
  • multi-enzyme complex
  • protein biosynthesis

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics
  • Clinical Biochemistry
  • Cell Biology

Cite this

Structural organization of high-Mr mammalian aminoacyl-tRNA synthetases - Comparison of multi-enzyme complexes from different sources. / Danga, Chi V.; Dang, Chuan V.

In: Molecular and Cellular Biochemistry, Vol. 63, No. 2, 09.1984, p. 131-136.

Research output: Contribution to journalArticle

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