The polyanion-binding domain of cytoplasmic Lys-tRNA synthetase from Saccharomyces cerevisiae is not essential for cell viability.

doi:10.1111/j.1432-1033.1992.tb17012.x

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Article

The polyanion-binding domain of cytoplasmic Lys-tRNA synthetase from Saccharomyces cerevisiae is not essential for cell viability.

European journal of biochemistry - 1 Jul 1992

Martinez R, Mirande M

Abstract excerpt

Cytoplasmic Lys-tRNA synthetase (LysRS) from Saccharomyces cerevisiae is a dimeric enzyme made up of identical subunits of 68 kDa. By limited proteolysis, this enzyme can be converted to a truncated dimer without loss of activity. Whereas the native enzyme strongly interacts with polyanionic carriers, the modified form displays reduced binding properties. KRS1 is the structural gene for yeast cytoplasmic LysRS....

Topics

Alleles
Amino Acid Sequence
Base Sequence
Chromosome Deletion
Chromosomes, Fungal
Cytoplasm
Genes, Fungal
Kinetics
Lysine-tRNA Ligase
Macromolecular Substances
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutagenesis, Site-Directed

Oligodeoxyribonucleotides

Pancreatic Elastase

Plasmids

Protein Conformation

Restriction Mapping

Saccharomyces cerevisiae

Source

Open in PubMed

Identifiers

PMID: 1628641
DOI: 10.1111/j.1432-1033.1992.tb17012.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1628641-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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