Molecular Dissection of a Protein SopB Essential for F Plasmid Partition
نویسندگان
چکیده
منابع مشابه
Insight into F plasmid DNA segregation revealed by structures of SopB and SopB–DNA complexes
Accurate DNA segregation is essential for genome transmission. Segregation of the prototypical F plasmid requires the centromere-binding protein SopB, the NTPase SopA and the sopC centromere. SopB displays an intriguing range of DNA-binding properties essential for partition; it binds sopC to form a partition complex, which recruits SopA, and it also coats DNA to prevent non-specific SopA-DNA i...
متن کاملMini-F protein that binds to a unique region for partition of mini-F plasmid DNA.
A mini-F-coded protein, named F2 protein, binds specifically to mini-F DNA. This protein has a molecular weight of 37,000 and is coded by the A2 segment of the mini-F genome (47.3 to 49.4 kilobases on the F coordinate map). The binding site is located also in the A2 segment of mini-F. This binding site is lost by spontaneous deletion when the A2 segment alone, but not A2 together with its neigh...
متن کاملLocalization of F plasmid SopB protein to positions near the poles of Escherichia coli cells.
The subcellular localization of the SopB protein, which is encoded by the Escherichia coli F plasmid and is involved in the partition of the single-copy plasmid, was directly visualized through the expression of the protein fused to the jellyfish green fluorescent protein (GFP). The fusion protein, but not GFP itself, was found to localize to positions close but not at the poles of exponentiall...
متن کاملTwelve 43-base-pair repeats map in a cis-acting region essential for partition of plasmid mini-F.
The nucleotide sequence of the DNA region involved in partitioning of plasmid mini-F has been determined. The sequence consists of 12 direct tandemly arranged repeats of 43 base pairs (the two flanking repeats, 43 plus 1 base pairs) with extensive homology to each other. Each repeat contains an additional inverted repeat of 7 base pairs.
متن کاملDissection of the ATPase active site of P1 ParA reveals multiple active forms essential for plasmid partition.
The segregation, or partition, of bacterial plasmids is driven by the action of plasmid-encoded partition ATPases, which work to position plasmids inside the cell. The most common type of partition ATPase, generally called ParA, is represented by the P1 plasmid ParA protein. ParA interacts with P1 ParB (the site-specific DNA binding protein that recognizes the parS partition site), and interact...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1996
ISSN: 0021-9258
DOI: 10.1074/jbc.271.29.17469