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PMID: 6746733 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

The eucaryotic aminoacyl-tRNA synthetase complex: suggestions for its structure and function.

The Journal of cell biology ·Vol. 99 ·No. 2 ·1984-08-00 ·Pages 373-7

Deutscher MP

Abstract

Aminoacyl-tRNA synthetases from eucaryotic cells generally are isolated as high molecular weight complexes comprised of multiple synthetase activities, and often containing other components as well. A model is proposed for the synthetase complex in which hydrophobic extensions on the proteins serve to maintain them in their high molecular weight form, but are not needed for catalytic activity. The structural similarity of these enzymes to certain membrane-bound proteins, and its implications for synthetase localization and function in vivo, are discussed.

MeSH Terms
Amino Acyl-tRNA Synthetases/metabolism Animals Cells/enzymology Eukaryotic Cells/enzymology Female Humans Liver/enzymology Models, Genetic Multienzyme Complexes/metabolism Placenta/enzymology Pregnancy Protein Conformation Reticulocytes/enzymology
Chemicals
Multienzyme Complexes Amino Acyl-tRNA Synthetases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Deutscher M P
References (58)
58 references, click to expand
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.99.2.373
Published
1984-08-00
Pages
373-7
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2113280
Subset
IM
Grants
NIGMS NIH HHS · GM16317 · United States
External Links
PubMed source DOI: 10.1083/jcb.99.2.373 PMC Full Text View journal details
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