Evolutionary Comparisons of RecA-Like Proteins Across All Major Kingdoms of Living Organisms |
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Authors: | Volker Brendel Luciano Brocchieri Steven J Sandler Alvin J Clark Samuel Karlin |
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Institution: | (1) Department of Mathematics, Stanford University, Stanford, CA 94305-2125, USA, US;(2) Department of Molecular and Cell Biology, Division of Genetics, University of California, Berkeley, Berkeley, CA 94720-3202, USA, US |
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Abstract: | Protein sequences with similarities to Escherichia coli RecA were compared across the major kingdoms of eubacteria, archaebacteria, and eukaryotes. The archaeal sequences branch
monophyletically and are most closely related to the eukaryotic paralogous Rad51 and Dmc1 groups. A multiple alignment of
the sequences suggests a modular structure of RecA-like proteins consisting of distinct segments, some of which are conserved
only within subgroups of sequences. The eukaryotic and archaeal sequences share an N-terminal domain which may play a role
in interactions with other factors and nucleic acids. Several positions in the alignment blocks are highly conserved within
the eubacteria as one group and within the eukaryotes and archaebacteria as a second group, but compared between the groups
these positions display nonconservative amino acid substitutions. Conservation within the RecA-like core domain identifies
possible key residues involved in ATP-induced conformational changes. We propose that RecA-like proteins derive evolutionarily
from an assortment of independent domains and that the functional homologs of RecA in noneubacteria comprise an array of RecA-like
proteins acting in series or cooperatively.
Received: 25 October 1996 / Accepted: 31 December 1996 |
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Keywords: | : Protein domains — RecA-like proteins — Multiple sequence alignment — SAPS program — SSPA program |
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