In:
Protein Science, Wiley, Vol. 11, No. 10 ( 2002-10), p. 2370-2381
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.
Type of Medium:
Online Resource
ISSN:
0961-8368
,
1469-896X
Language:
English
Publisher:
Wiley
Publication Date:
2002
detail.hit.zdb_id:
2000025-X
SSG:
12
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