Proc Natl Acad Sci U S A. 1991 Oct 1;88(19):8387-91.

Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase.

Sanni A, Walter P, Boulanger Y, Ebel JP, Fasiolo F.

Source

Institut de Biologie Molecularie et Cellulaire du Centre National de la Recherche Scientifique, Laboratoire de Biochimie, Strasbourg, France.

Abstract

Phenylalanyl-tRNA synthetases [L-phenylalanine:tRNAPhe ligase (AMP-forming), EC 6.1.1.20] from Escherichia coli, yeast cytoplasm, and mammalian cytoplasm have an unusual conserved alpha 2 beta 2 quaternary structure that is shared by only one other aminoacyl-tRNA synthetase. Both subunits are required for activity. We show here that a single mitochondrial polypeptide from Saccharomyces cerevisiae is an active phenylalanyl-tRNA synthetase. This protein (the MSF1 gene product) is active as a monomer. It has all three characteristic sequence motifs of the class II aminoacyl-tRNA synthetases, and its activity may result from the recruitment of additional sequences into an alpha-subunit-like structure.

PMID:: 1924298; [PubMed - indexed for MEDLINE]
PMCID:: PMC52513

Free PMC Article

LinkOut - more resources

Full Text Sources

Molecular Biology Databases

Saccharomyces Genome Database

Research Materials

online strain list - StrainInfo

Supplemental Content

Save items

Related citations in PubMed

Isolation and characterization of the yeast gene coding for the alpha subunit of mitochondrial phenylalanyl-tRNA synthetase. [J Biol Chem. 1987]
Isolation and characterization of the yeast gene coding for the alpha subunit of mitochondrial phenylalanyl-tRNA synthetase.
Koerner TJ, Myers AM, Lee S, Tzagoloff A. J Biol Chem. 1987 Mar 15; 262(8):3690-6.
Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site. [Biochemistry. 1996]
Conservation in evolution for a small monomeric phenylalanyl-tRNA synthetase of the tRNA(Phe) recognition nucleotides and initial aminoacylation site.
Aphasizhev R, Senger B, Rengers JU, Sprinzl M, Walter P, Nussbaum G, Fasiolo F. Biochemistry. 1996 Jan 9; 35(1):117-23.
Structure and evolution of a group of related aminoacyl-tRNA synthetases. [J Mol Biol. 1991]
Structure and evolution of a group of related aminoacyl-tRNA synthetases.
Gatti DL, Tzagoloff A. J Mol Biol. 1991 Apr 5; 218(3):557-68.
Review Structure, function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic code. [J Mol Evol. 1995]
Review Structure, function and evolution of seryl-tRNA synthetases: implications for the evolution of aminoacyl-tRNA synthetases and the genetic code.
Härtlein M, Cusack S. J Mol Evol. 1995 May; 40(5):519-30.
Review Understanding structural relationships in proteins of unsolved three-dimensional structure. [Proteins. 1990]
Review Understanding structural relationships in proteins of unsolved three-dimensional structure.
Burbaum JJ, Starzyk RM, Schimmel P. Proteins. 1990; 7(2):99-111.

See reviews... See all...

Cited by 12 PubMed Central articles

Structural Aspects of Phenylalanylation and Quality Control in Three Major Forms of Phenylalanyl-tRNA Synthetase. [J Amino Acids. 2010]
Structural Aspects of Phenylalanylation and Quality Control in Three Major Forms of Phenylalanyl-tRNA Synthetase.
Klipcan L, Finarov I, Moor N, Safro MG. J Amino Acids. 2010; 2010:983503. Epub 2010 Jun 27.
Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP. [Protein Sci. 2011]
Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP.
Mermershtain I, Finarov I, Klipcan L, Kessler N, Rozenberg H, Safro MG. Protein Sci. 2011 Jan; 20(1):160-7.
Pathogenic mechanism of a human mitochondrial tRNAPhe mutation associated with myoclonic epilepsy with ragged red fibers syndrome. [Proc Natl Acad Sci U S A. 2007]
Pathogenic mechanism of a human mitochondrial tRNAPhe mutation associated with myoclonic epilepsy with ragged red fibers syndrome.
Ling J, Roy H, Qin D, Rubio MA, Alfonzo JD, Fredrick K, Ibba M. Proc Natl Acad Sci U S A. 2007 Sep 25; 104(39):15299-304. Epub 2007 Sep 18.

See all...

Related information

Related Citations
Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
BioSystems
Pathways and biological systems (BioSystems) that cite the current articles. Citations are from the BioSystems source databases (KEGG and BioCyc).
Gene
Gene records that cite the current articles. Citations in Gene are added manually by NCBI or imported from outside public resources.
HomoloGene
HomoloGene clusters of homologous genes and sequences that cite the current articles. These are references on the Gene and sequence records in the HomoloGene entry.
Nucleotide (RefSeq)
NCBI nucleotide Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.
Nucleotide (Weighted)
Nucleotide records associated with the current articles through the Gene database. These are the related sequences on the Gene record that are added manually by NCBI.
Protein (RefSeq)
NCBI protein Reference Sequences (RefSeqs) that are cited in the current articles, included in the corresponding Gene Reference into Function, or that include the PubMed articles as references.
Protein (Weighted)
Protein records associated with the current articles through related Gene database records. These are the related sequences on the Gene record that are added manually by NCBI.
References for this PMC Article
Citation referenced in PubMed article. Only valid for PubMed citations that are also in PMC.
Taxonomy via GenBank
Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).
Domains
Conserved Domain Database (CDD) records that cite the current articles. Citations are from the CDD source database records (PFAM, SMART).
Protein
Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.
GEO Profiles
Gene Expression Omnibus (GEO) Profiles of molecular abundance data. The current articles are references on the Gene record associated with the GEO profile.
Free in PMC
Free full text articles in PMC
Cited in PMC
Full-text articles in the PubMed Central Database that cite the current articles.
Cited in Books
NCBI Bookshelf books that cite the current articles.

Recent activity

Clear Turn Off Turn On

Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccha...
Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase.
Proc Natl Acad Sci U S A. 1991 Oct 1 ;88(19):8387-91.

PubMed

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

PubMed

Result Filters

Display Settings:

Send to:

Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase.

Source

Abstract

Publication Types, MeSH Terms, Substances

Publication Types

MeSH Terms

Substances

LinkOut - more resources

Full Text Sources

Molecular Biology Databases

Research Materials

Supplemental Content

Save items

Related citations in PubMed

Cited by 12 PubMed Central articles

Related information

Recent activity

Simple NCBI Directory

Getting Started

Resources

Popular

Featured

NCBI Information