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PrfA protein of Bacillus species: Prediction and demonstration of endonuclease activity on DNA
Author(s) -
Rigden Daniel J.,
Setlow Peter,
Setlow Barbara,
Bagyan Irina,
Stein Richard A.,
Jedrzejas Mark J.
Publication year - 2002
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.0216802
Subject(s) - dna , circular bacterial chromosome , dna supercoil , plasmid , endonuclease , in vitro recombination , restriction enzyme , biology , mutant , recombinant dna , homology (biology) , gene , chemistry , biochemistry , dna replication , genetics , peptide sequence , molecular cloning
Abstract The prfA gene product of Gram‐positive bacteria is unusual in being implicated in several cellular processes; cell wall synthesis, chromosome segregation, and DNA recombination and repair. However, no homology of PrfA with other proteins has been evident. Here we report a structural relationship between PrfA and the restriction enzyme Pvu II, and thereby produce models that predict that PrfA binds DNA. Indeed, wild‐type Bacillus stearothermophilus PrfA, but not a catalytic site mutant, nicked one strand of supercoiled plasmid templates leaving 5′‐phosphate and 3′‐hydroxyl termini. This activity, much lower on linear or relaxed circular double‐stranded DNA or on single‐stranded DNA, is consistent with a role for this protein in chromosome segregation, DNA recombination, or DNA repair.