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PMID: 6832143 Published · ppublish English Journal Article

Activity patterns of aminoacyl-tRNA synthetases, tRNA methylases, arginyltransferase and tubulin: tyrosine ligase during development and ageing of Caenorhabditis elegans.

European journal of biochemistry ·Vol. 131 ·No. 1 ·1983-03-01 ·Pages 231-4

Gabius HJ, Graupner G, Cramer F

Abstract

As a step in the characterization of development and ageing in the nematode Caenorhabditis elegans, the activities of different groups of enzymes that supposedly exert modulating functions in and after protein synthesis have been determined. From embryonic (E), the four juvenile larval stages (L1-L4) and the gravid adult (A,A+), the selection of defined developmental stages extends to two different preparations of aged nematodes (S10, S12). Some aminoacyl-tRNA synthetase activities remain nearly unchanged in all stages up to the adult, some increase continuously during the larval stages and the remaining activities show stage-specific alterations. Upon ageing all activities except the one for tryptophan decrease sharply, tRNA methylase activities increase from E to L4, decrease from L4 to adult and to aged nematodes with only qualitative alterations in substrate specificity. The activity of tubulin: tyrosine ligase exhibits a parallel pattern, while arginyltransferase activity has a plateau between L2 and L4. The results are consistent with the idea of a modulation of protein synthesis and other cellular processes by quantitative activity changes during development and ageing.

MeSH Terms
Acyltransferases/metabolism Amino Acids/metabolism Amino Acyl-tRNA Synthetases/metabolism Aminoacyltransferases Animals Caenorhabditis/enzymology,growth & development Peptide Synthases/metabolism Protein Processing, Post-Translational Substrate Specificity tRNA Methyltransferases/metabolism
Chemicals
Amino Acids tRNA Methyltransferases Acyltransferases Aminoacyltransferases arginyltransferase Amino Acyl-tRNA Synthetases Peptide Synthases tyrosyltubulin ligase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Gabius H J
Graupner G
Cramer F
Article Info
Journal
European journal of biochemistry
Abbr.
Eur J Biochem
ISSN
0014-2956
Published
1983-03-01
Pages
231-4
Language
English
Region
England
NLM ID
0107600
Subset
IM
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