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Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase

Nature volume 306, pages 441–447 (1983)Cite this article

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 sizes of aminoacyl tRNA synthetases.

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Authors and Affiliations

  1. Department of Biology, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA

    Maria Jasin, Lynne Regan & Paul Schimmel

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  1. Maria Jasin
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  2. Lynne Regan
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  3. Paul Schimmel
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Jasin, M., Regan, L. & Schimmel, P. Modular arrangement of functional domains along the sequence of an aminoacyl tRNA synthetase. Nature 306, 441–447 (1983). https://doi.org/10.1038/306441a0

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