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Mammalian tryptophanyl-tRNA synthetases
1Engelhardt Institute of Molecular Biology, Moscow, Russia.
Biochimie
|January 1, 1993
Summary
Mammalian tryptophanyl-tRNA synthetases (TrpRS) are Zn(2+)-dependent enzymes with unique features like an N-terminal extension. TrpRS activity increases with interferon gamma and is overproduced in Ruminantia pancreas.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Aminoacyl-tRNA synthetases (aaRS) in higher organisms are less studied than prokaryotic/unicellular counterparts.
- Mammalian aaRS display unique features absent in bacterial or yeast enzymes.
- Tryptophanyl-tRNA synthetase (TrpRS) is a well-studied mammalian aaRS, a dimeric, class I, Zn(2+)-dependent enzyme.
Purpose of the Study:
- To summarize and discuss available data on mammalian Tryptophanyl-tRNA synthetases (TrpRS).
- To highlight unique characteristics of mammalian TrpRS compared to other organisms.
- To review TrpRS's role in interferon response and its overproduction in Ruminantia.
Main Methods:
- Literature review and data summarization.
- Comparative analysis of TrpRS sequences and properties across mammalian orders.
- Discussion of TrpRS gene regulation and expression patterns.
Main Results:
- Mammalian TrpRS possess a long N-terminal extension not found in bacterial TrpRS.
- Human TrpRS gene is interferon-responsive, with activity increasing after interferon gamma induction.
- TrpRS is notably overproduced in the pancreas of Ruminantia for unknown reasons.
Conclusions:
- Mammalian TrpRS exhibit distinct structural and regulatory features compared to their prokaryotic and unicellular eukaryotic homologs.
- The interferon-inducible nature of human TrpRS suggests a role in cellular defense mechanisms.
- Further research is needed to elucidate the reasons for TrpRS overproduction in Ruminantia pancreas.