期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 469, 期 4, 页码 1028-1033出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2015.12.099
关键词
Reactive oxygen species; Bacterioferritin comigratory protein; DNA-binding protein; DNA chaperone; Peroxiredoxin
资金
- ETRI research program [B0132-15-1001]
- National Research Foundation of Korea - Ministry of Science, ICT & Future Planning [NRF-2015R1C1A1A01053611]
Bacterioferritin comigratory protein (BCP) is a monomeric conformer acting as a putative thioldependent bacterial peroxidase, however molecular basis of DNA-protection via DNA-binding has not been clearly understood. In this study, we characterized the DNA binding properties of BCP using various lengths and differently shaped architectures of DNA. An electrophoretic mobility shift assay and electron microscopy analysis showed that recombinant TkBCP bound to DNA of a circular shape (double-stranded DNA and single-stranded DNA) and a linear shape (16-1000 bp) as well as various architectures of DNA. In addition, DNA protection experiments indicated that TkBCP can protect DNA against hyperthermal and oxidative stress by removing highly reactive oxygen species (ROS) or by protecting DNA from thermal degradation. Based on these results, we suggest that TkBCP is a multi-functional DNA-binding protein which has DNA chaperon and antioxidant functions. (C) 2015 Elsevier Inc. All rights reserved.
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