Work

PrfA protein of Bacillus species: Prediction and demonstration of endonuclease activity on DNA

Year: 2002

Type: article

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 PvuII, 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.

Source: Protein Science

DOI: 10.1110/ps.0216802

Authors: Daniel J. Rigden, Peter Setlow, Barbara Setlow, Irina Bagyan, Richard A. Stein, Mark J. Jedrzejas

Institutions: Embrapa, Embrapa Recursos Genéticos e Biotecnologia, UConn Health, University of Alabama at Birmingham

Language: English

Topic: Bacterial Genetics and Biotechnology

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funders: National Institute of General Medical Sciences, National Institute of Allergy and Infectious Diseases

Awards: G1197907232, DEGRADATION REACTIONS IN SPORE GERMINATION, STRUCTURAL STUDIES OF BACTERIAL HYALURONATE LYASE ENZYME, Degradation Reactions in Spore Germination