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. 1980 May;142(2):729–731. doi: 10.1128/jb.142.2.729-731.1980

Interspecies hybrid tryptophan synthase-modified beta 2 protein formed from separate folding regions of the beta monomer.

V Rocha, E F Brennan
PMCID: PMC294063  PMID: 6991487

Abstract

Escherichia coli and Serratia marcescens tryptophan synthase beta 2 protein (EC 4.2.1.20) was subjected to mild trypsin proteolysis. Two separate folding regions (domains) of the E. coli (EF1 and EF2) and the S. marcescens (SF1 and SF2) enzyme were shown to form interspecies hybrid reconstituted molecules [(EF1-SF2)2 and (SF1-EF2)2] and intraspecies reconstituted molecules [(EF1-EF2)2 and (SF1-SF2)2] with equal efficiency. The data suggest that structural regions, associated with beta monomer assembly, exist somewhere on the domain fragments and that these regions are conserved.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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