Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms

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...

Full description

Saved in:
Bibliographic Details
Published in:Journal of molecular evolution 1997-05, Vol.44 (5), p.528-541
Main Authors: Brendel, V, Brocchieri, L, Sandler, S J, Clark, A J, Karlin, S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Animals
Archaeal Proteins
Bacteria - genetics
Bacterial Proteins
Bacteriology
Cell Cycle Proteins
Consensus Sequence - genetics
Conserved Sequence - genetics
DNA-Binding Proteins - genetics
E coli
Escherichia coli
Escherichia coli Proteins
Eukaryotes
Evolution, Molecular
Evolutionary biology
Humans
Molecular Sequence Data
Nucleic acids
Organisms
Phylogeny
Proteins
Rad51 Recombinase
Rec A Recombinases - genetics
Sequence Alignment
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0022-2844
1432-1432
DOI:10.1007/pl00006177