Identification of a novel protein, PriB, in Klebsiella pneumoniae

doi:10.1016/j.bbrc.2010.12.023

中山醫學大學機構典藏 CSMUIR > 醫學科技學院 > 生物醫學科學學系暨碩士班 > 期刊論文 > Item 310902500/4332

Please use this identifier to cite or link to this item: https://ir.csmu.edu.tw:8080/ir/handle/310902500/4332

Title:	Identification of a novel protein, PriB, in Klebsiella pneumoniae
Authors:	Hui-Chuan Hsieh Cheng-Yang Huang
Contributors:	中山醫學大學生物醫學科學系
Keywords:	PriB SSB ssDNA binding PriA Primosome
Date:	2011-01-07
Issue Date:	2012-07-19T07:58:00Z (UTC)
ISSN:	0006-291X
Abstract:	PriB is a primosomal protein required for the reinitiation of replication in bacteria. Here, we report the identification and characterization of a novel PriB protein in Klebsiella pneumoniae (KPN_04595; KpPriB). Unlike the well-studied Escherichia coli PriB protein (EcPriB), which exists as a homodimer comprising 104-aa polypeptides, KpPriB forms a monomer of only 55 aa, due to the absence of the 49 aa N-terminus in KpPriB. Although this N-terminal region (1–49 aa) in EcPriB contains several important residues, such as K18, R34, and W47, which are crucial for ssDNA binding, we found that KpPriB binds ssDNA, but not ssRNA, with comparable affinity as that for EcPriB. Results from filter-binding assays demonstrate that the KpPriB–ssDNA interaction is cooperative and salt-sensitive. Substituting the residue K33 in KpPriB with alanine, the position corresponding to the classic ssDNA-binding residue K82 of EcPriB located in loop L45, significantly reduced ssDNA-binding activity and cooperativity. These results reveal that the 1–49 aa region of the classical PriB protein is unnecessary for ssDNA binding. On the basis of these findings, the structure–function relationships of KpPriB are discussed.
URI:	https://ir.csmu.edu.tw:8080/ir/handle/310902500/4332 http://dx.doi.org/10.1016/j.bbrc.2010.12.023
Relation:	Biochemical and Biophysical Research Communications Volume 404, Issue 1, 7 January 2011, Pages 546–551
Appears in Collections:	[生物醫學科學學系暨碩士班] 期刊論文

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