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Interactions of the parA protein in the partition of DNA during bacterial cell division / Qiuling Zong

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Identifier	Thesis 1513
Author	Zong, Qiuling
Title	Interactions of the parA protein in the partition of DNA during bacterial cell division / Qiuling Zong
Publisher	Central Connecticut State University
Date	1997
Resource Type	Master's Thesis
Notes	The prophage of bacteriophage P1 is a unit copy plasmid, stable in Escherichia coli during cell division due to its partition system. The active P1 partition system consists of two genes, parA and parB, and a cis-site, parS. ParS contains all of the information required in cis to direct the segregation of the plasmid. Par B protein recognizes the parS sequence and binds to it to form a large protein-DNA complex. The function of parA protein in P1 partition is less well understood. It is known to have autoregulatory activity and ATPase activity in vitro. Both its autoregulatory and ATPase are stimulated by parB. Current models of partition suggest that the replicated plasmid copies attach to a specific host receptor on the cell division plane. It is postulated that parA is associated with parB-parS complex and interacts with host receptor protein. To find the putative host receptor protein that interacts with parA, we have fused the parA gene with a maltose-binding protein (MBP) gene in a pMAL cloning vector. The Ptac promoter will allow us to express large amounts of the MBP-ParA fusion protein. This fused protein, bound to an amylose column, will be used to isolate the cell membrane protein which associates with parA. A parA-host receptor complex can be cleaved at the MBP-ParA fusion site with the specific protease factor Xa. Proteins isolated by affinity with parA will be tested for their role in partition.
Subject	DNA-protein interactions
Department	Department of Biological Sciences
Advisor	Martin-Troy, Kathy
Type	Text
Digital Format	application/pdf
Language	eng
OCLC number	40103268
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