Arc1p is required for cytoplasmic confinement of synthetases and tRNA

In yeast, Arc1p interacts with ScMetRS and ScGluRS and operates as a tRNA-Interacting Factor (tIF) in trans of these two synthetases. Its N-terminal domain (N-Arc1p) binds the two synthetases and its C-terminal domain is an EMAPII-like domain organized around an OB-fold-based tIF. ARC1 is not an ess...

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Veröffentlicht in:	Molecular and cellular biochemistry 2007-06, Vol.300 (1-2), p.47-59
Hauptverfasser:	Golinelli-Cohen, Marie-Pierre, Mirande, Marc
Format:	Artikel
Sprache:	eng
Schlagworte:	Antigens, Neoplasm - chemistry Arc1p Catalysis Clonal deletion Cytoplasm - enzymology Discrete functions Gene deletion Genotype & phenotype Glutamate-tRNA Ligase - metabolism Growth rate Humans Lethality Life Sciences Localization Methionine-tRNA Ligase - metabolism Methionyl-tRNA synthetase Microbial Viability Mitochondrial Proteins Models, Biological p43 Peptide Elongation Factor Tu - chemistry Phenotypes Protein Structure, Tertiary Proteins RNA, Transfer - metabolism RNA-Binding Proteins - chemistry RNA-Binding Proteins - metabolism Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Solutions Subcellular organization Transfer RNA tRNA tRNA-Interacting Factor Yeasts
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