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Science 26 March 1993:
Vol. 259. no. 5103, pp. 1892 - 1896
DOI: 10.1126/science.8456313
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Articles

Science, Vol 259, Issue 5103, 1892-1896
Copyright © 1993 by American Association for the Advancement of Science

articles

Structural relationship of bacterial RecA proteins to recombination proteins from bacteriophage T4 and yeast

RM Story, DK Bishop, N Kleckner, and TA Steitz

Department of Molecular Biophysics, Yale University, New Haven, CT 06511.

RecA protein is essential in eubacteria for homologous recombination and promotes the homologous pairing and strand exchange of DNA molecules in vitro. Recombination proteins with weak sequence similarity to bacterial RecA proteins have been identified in bacteriophage T4, yeast, and other higher organisms. Analysis of the primary sequence relationships of DMC1 from Saccharomyces cerevisiae and UvsX of T4 relative to the three-dimensional structure of RecA from Escherichia coli suggests that both proteins are structural homologs of bacterial RecA proteins. This analysis argues that proteins in this group are members of a single family that diverged from a common ancestor that existed prior to the divergence of prokaryotes and eukaryotes.


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J. Immunol. 162, 911-919
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okra and spindle-B encode components of the RAD52 DNA repair pathway and affect meiosis and patterning in Drosophila oogenesis.
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RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange.
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RecA-like proteins are components of early meiotic nodules in lily.
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The DNA Binding Site(s) of the Escherichia coli RecA Protein.
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Roles for two RecA homologs in promoting meiotic chromosome synapsis..
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Homotypic and heterotypic protein associations control Rad51 function in double-strand break repair..
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Catalysis of ATP-dependent homologous DNA pairing and strand exchange by yeast RAD51 protein.
P Sung (1994)
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The Sep1 strand exchange protein from Saccharomyces cerevisiae promotes a paranemic joint between homologous DNA molecules..
J Chen, R Kanaar, and N R Cozzarelli (1994)
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