Senger B, Despons L, Walter P, Jakubowski H, Fasiolo F
Yeast cytoplasmic and mitochondrial methionyl-tRNA synthetases: two structural frameworks for identical functions Article de journal
Dans: J Mol Biol, vol. 311, no. 1, p. 205-216, 2001, ISBN: 11469869, (0022-2836 Journal Article).
Résumé | Liens | BibTeX | Étiquettes: Acylation Amino Acid Sequence Binding Sites Coenzyme A/metabolism Comparative Study Cysteine/genetics/metabolism Cytoplasm/*enzymology Genes, Fungal/genetics Genetic Complementation Test Homocysteine/genetics/metabolism Kinetics Methionine/metabolism Methionine-tRNA Ligase/*chemistry/genetics/*metabolism Mitochondria/*enzymology Molecular Sequence Data Mutation/genetics Protein Transport RNA, Met/genetics/metabolism Saccharomyces cerevisiae/cytology/*enzymology/genetics Sequence Alignment Structure-Activity Relationship Support, Non-P.H.S. Zinc/metabolism Zinc Fingers/genetics/physiology, Non-U.S. Gov't Support, Transfer, U.S. Gov't, Unité ARN
@article{,
title = {Yeast cytoplasmic and mitochondrial methionyl-tRNA synthetases: two structural frameworks for identical functions},
author = {B Senger and L Despons and P Walter and H Jakubowski and F Fasiolo},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=11469869},
isbn = {11469869},
year = {2001},
date = {2001-01-01},
journal = {J Mol Biol},
volume = {311},
number = {1},
pages = {205-216},
abstract = {The yeast Saccharomyces cerevisiae possesses two methionyl-tRNA synthetases (MetRS), one in the cytoplasm and the other in mitochondria. The cytoplasmic MetRS has a zinc-finger motif of the type Cys-X(2)-Cys-X(9)-Cys-X(2)-Cys in an insertion domain that divides the nucleotide-binding fold into two halves, whereas no such motif is present in the mitochondrial MetRS. Here, we show that tightly bound zinc atom is present in the cytoplasmic MetRS but not in the mitochondrial MetRS. To test whether the presence of a zinc-binding site is required for cytoplasmic functions of MetRS, we constructed a yeast strain in which cytoplasmic MetRS gene was inactivated and the mitochondrial MetRS gene was expressed in the cytoplasm. Provided that methionine-accepting tRNA is overexpressed, this strain was viable, indicating that mitochondrial MetRS was able to aminoacylate tRNA(Met) in the cytoplasm. Site-directed mutagenesis demonstrated that the zinc domain was required for the stability and consequently for the activity of cytoplasmic MetRS. Mitochondrial MetRS, like cytoplasmic MetRS, supported homocysteine editing in vivo in the yeast cytoplasm. Both MetRSs catalyzed homocysteine editing and aminoacylation of coenzyme A in vitro. Thus, identical synthetic and editing functions can be carried out in different structural frameworks of cytoplasmic and mitochondrial MetRSs.},
note = {0022-2836
Journal Article},
keywords = {Acylation Amino Acid Sequence Binding Sites Coenzyme A/metabolism Comparative Study Cysteine/genetics/metabolism Cytoplasm/*enzymology Genes, Fungal/genetics Genetic Complementation Test Homocysteine/genetics/metabolism Kinetics Methionine/metabolism Methionine-tRNA Ligase/*chemistry/genetics/*metabolism Mitochondria/*enzymology Molecular Sequence Data Mutation/genetics Protein Transport RNA, Met/genetics/metabolism Saccharomyces cerevisiae/cytology/*enzymology/genetics Sequence Alignment Structure-Activity Relationship Support, Non-P.H.S. Zinc/metabolism Zinc Fingers/genetics/physiology, Non-U.S. Gov't Support, Transfer, U.S. Gov't, Unité ARN},
pubstate = {published},
tppubtype = {article}
}