Words similar to exo
Example sentences for: exo
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Studies in Escherichia coli have shown that, although RecA is the principle protein involved in pairing and strand exchange, unrelated proteins, that have a much more restrictive phyletic distribution, can also promote similar reactions in a RecA dependent or RecA-independent manner [ 3 ] . These alternative or additional mediators of homologous recombination include the well-characterized prophage RecT, phage λ Redβ and phage P22 ERF proteins [ 4 5 ] . Similarly, in yeast and vertebrates, the RAD52 protein is involved in the pairing and strand exchange reaction and can promote recombination in a RAD51 (the eukaryotic RecA homolog)-dependent or independent manner [ 6 ] . The RecT protein works in conjunction with the RecE-nuclease [ 7 ] and was initially described in genetic studies on the complemention of mutations in the RecBCD pathway of DNA repair [ 8 9 10 ] . Biochemically, RecT has been shown to bind single-stranded (ss) DNA 3' overhang regions generated by the RecE nuclease, and promote strand exchange between homologous DNA partners by assisting the pairing of complementary single-stranded regions [ 4 10 ] . The reaction catalyzed by the RecT/RecE system is similar to that described for the phage λ exonuclease (exo/Redβ) and the single-strand annealing protein Redβ.
The similarity between these two systems is further extended by the observation that the RecT/E system can complement mutations in the λ exo/Redβ system [ 10 12 ] . In eukaryotes, RAD52 protein has been shown to exhibit properties similar to those of RecT and Redβ proteins: it binds ssDNA and promotes strand exchange via the pairing of complementary single strands [ 6 13 ] . In vitro studies on quaternary structures have shown that the single strand annealing proteins (SSAPs), RecT, Redβ, ERF and RAD52, form similar helical super-structures [ 14 15 16 17 ] . This has led to the proposal that RecT, Redβ, ERF and the eukaryotic RAD52 function in an analogous fashion, and even are "structural homologs" [ 14 ] .
No amino acid changes were identified within the proofreading (Exo) domains.
The replicative polymerase of herpes simplex virus (HSV) is comprised of catalytic (Pol) and processivity subunits (UL42) [ 9 11 ] . HSV Pol is responsible, in concert with other viral proteins, for regulating the fidelity of DNA replication by selecting the correct nucleotides for incorporation and by proofreading or editing mispaired nucleotides [ 20 ] . The Pol subunit contains intrinsic 3'-5' exonuclease activity [ 14 15 16 ] and the N-terminal region of the polypeptide encoding this function is highly conserved in other polymerases, containing three segments referred to as Exo motifs [ 3 26 ] .
Some sequence entries represented the same protein, called by different names or isolated in different screens, including many entries for huAPE1, Drosophila Rrp 1 protein (~40% identical to the mammalian APE1 in the C-terminal third of the protein), Xth from E. coli , and counterparts of this and exodeoxyribonuclease (exo A) sequences from many bacteria, which are about 25% identical to mammalian APE1.
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