Domainal evolution of a prokaryotic DNA repair protein and its relationship to active-transport proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1986-10

AUTHORS

R. F. Doolittle, M. S. Johnson, I. Husain, B. Van Houten, D. C. Thomas, A. Sancar

ABSTRACT

The ABC excision nuclease of Escherichia coll is an ATP-depen-dent DNA repair enzyme composed of three protein subunits, UvrA, UvrB and UvrC. The DNA sequences of all three genes have been reported1–3. UvrA, the component that binds directly to the DNA, and UvrB, which attaches itself to the UvrA-DNA complex, both contain consensus sequences thought to be diagnostic of ATP-binding sites4, although the UvrC sequence does not. We now report that a computer analysis of the UvrA sequence has revealed an unusual series of internal duplications centering around putative metal-binding sites which may be involved in the interaction with DNA. We also find a strong evolutionary relationship to a family of prokaryotic membrane-associated active-transport proteins. More... »

PAGES

451-453

References to SciGraph publications

  • 1985-02. Aligning amino acid sequences: Comparison of commonly used methods in JOURNAL OF MOLECULAR EVOLUTION
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/323451a0

    DOI

    http://dx.doi.org/10.1038/323451a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1010798675

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/3762695


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