Abstract
Gene deletions show that much of Escherichia coli alanine tRNA synthetase is dispensable for each of three activities and that these activities appear to require specific domains arranged linearly along the polypeptide. Thus, variable fusions of extra polypeptide domains to a catalytic core may account for the diverse of aminoacyl tRNA synthetases.
Publication types
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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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Adenosine Triphosphate / metabolism
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Alanine-tRNA Ligase / genetics*
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Alanine-tRNA Ligase / metabolism
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Amino Acyl-tRNA Synthetases / genetics*
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Binding Sites
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Chromosome Deletion
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Escherichia coli / enzymology*
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Genes
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Macromolecular Substances
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Protein Conformation
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RNA, Transfer / metabolism
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Structure-Activity Relationship
Substances
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Macromolecular Substances
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Adenosine Triphosphate
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RNA, Transfer
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Amino Acyl-tRNA Synthetases
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Alanine-tRNA Ligase