Tripartite functional assembly of a large class I aminoacyl tRNA synthetase.
A 939-amino acid monomeric class I tRNA synthetase has been split into three inactive peptides. The three peptides spontaneously assemble in vivo to reconstitute active protein. Active tripartite complexes were demonstrated in vitro. The tripartite assembly of this synthetase increases by several-fold the size of a polypeptide that has been demonstrated to be assembled from more than two constituent pieces. The results indicate that contemporary single-chain tRNA synthetases or other large proteins could in principle develop from intermediates composed of non-covalent assemblages of multiple peptides.
Shiba
K
K
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
Schimmel
P
P
D000595:Amino Acid Sequence; D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D015153:Blotting, Western; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005816:Genetic Complementation Test; D007533:Isoleucine-tRNA Ligase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010957:Plasmids; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
D046911:Macromolecular Substances; D000604:Amino Acyl-tRNA Synthetases; D007533:Isoleucine-tRNA Ligase