Journal
JOURNAL OF BACTERIOLOGY
Volume 186, Issue 9, Pages 2717-2723Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.186.9.2717-2723.2004
Keywords
-
Categories
Funding
- NIAID NIH HHS [R01 AI033537, 5T32 AI 49820, T32 AI049820, AI 33537] Funding Source: Medline
- NIGMS NIH HHS [R01 GM031685, GM 31685] Funding Source: Medline
Ask authors/readers for more resources
A minireplicon of plasmid pXO2 of Bacillus anthracis was isolated by molecular cloning in Escherichia coli and shown to replicate in B. anthracis, Bacillus cereus, and Bacillus subtilis. The pXO2 replicon included (i) an open reading frame encoding the putative RepS replication initiation protein and (ii) the putative origin of replication. The RepS protein was expressed as a fusion with the maltose binding protein (MBP) at its amino-terminal end and purified by affinity chromatography. Electrophoretic mobility shift assays showed that the purified MBP-RepS protein bound specifically to a 60-bp region corresponding to the putative origin of replication of pXO2 located immediately downstream of the RepS open reading frame. Competition DNA binding experiments showed that the 5' and central regions of the putative origin were important for RepS binding. MBP-RepS also bound nonspecifically to single-stranded DNA with a lower affinity.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available