Procedure for production of hybrid genes and proteins and its use in assessing significance of amino acid differences in homologous tryptophan synthetase alpha polypeptides.
- 1 April 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (4) , 2169-2173
- https://doi.org/10.1073/pnas.78.4.2169
Abstract
Hybrid tryptophan synthetase .alpha. and .beta. polypeptides were produced by genetic recombination between the trpB-trpA regions of Escherichia coli and Salmonella typhimurium contained on compatible, multicopy plasmids. Intragenic recombination was decreased but still evident in recA cells. Genetic exchange occurred at many sites within trpA, but every recombinant gene produced a functional .alpha. polypeptide despite many amino acid differences from one or the other of the parental polypeptides. The 5 hybrid tryptophan synthetase .alpha. subunits examined resembled the parental polypeptides in catalytic function but differed in thermostability. The stability differences suggest that, as amino acid changes occurred in these proteins during the course of evolution, subsequent changes were limited to those that would allow retention of a desired protein conformation.This publication has 18 references indexed in Scilit:
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