Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Amino Acyl-tRNA Synthetases / chemistry
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Amino Acyl-tRNA Synthetases / genetics*
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Amino Acyl-tRNA Synthetases / isolation & purification
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Blotting, Western
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Escherichia coli / enzymology
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Escherichia coli / genetics
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Genetic Complementation Test
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Isoleucine-tRNA Ligase / genetics*
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Isoleucine-tRNA Ligase / isolation & purification
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Isoleucine-tRNA Ligase / metabolism
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Kinetics
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Macromolecular Substances
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Molecular Sequence Data
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Molecular Weight
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Plasmids
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Protein Conformation
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Sequence Homology, Amino Acid
Substances
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Macromolecular Substances
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Amino Acyl-tRNA Synthetases
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Isoleucine-tRNA Ligase