Evolution of aminoacyl-tRNA synthetase quaternary structure and activity: Saccharomyces cerevisiae mitochondrial phenylalanyl-tRNA synthetase.
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.
Institut de Biologie Molecularie et Cellulaire du Centre National de la Recherche Scientifique, Laboratoire de Biochimie, Strasbourg, France.
A
A
Sanni
P
P
Walter
Y
Y
Boulanger
J P
JP
Ebel
F
F
Fasiolo
D000595:Amino Acid Sequence; D001483:Base Sequence; D005075:Biological Evolution; D004252:DNA Mutational Analysis; D004926:Escherichia coli / Q000235:genetics; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure; D005800:Genes, Fungal; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D009841:Oligonucleotides / Q000737:chemistry; D010652:Phenylalanine-tRNA Ligase / Q000235:genetics* / Q000378:metabolism / Q000648:ultrastructure; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D015183:Restriction Mapping; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D016415:Sequence Alignment; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D005656:Fungal Proteins; D009841:Oligonucleotides; D011993:Recombinant Fusion Proteins; D010652:Phenylalanine-tRNA Ligase