JKMRS Volume 20, No 2, pp 36; Secondary structure analysis of ... | |
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2016년 06월 20일 / 조회수: 555 | |
Secondary structure analysis of MRA1997 from Mycobacterium tuberculosis and characterization of DNA binding property
Hyo Jung Kim1, Ki-Young Lee1, Yena Kim1, Ae-Ran Kwon2, and Bong-Jin Lee1*
1Research Institute of Pharmaceutical sciences, College of Pharmacy, Seoul National University, Gwanak-gu, Seoul 151-742, Korea 2Department of Herbal Skin Care, College of Herbal Bio-industry, Daegu Haany University, Gyeongsan 712-715, Korea
Received Mar 19, 2016; Revised Apr 25, 2016; Accepted May 7, 2016
Abstract MRA1997 is a highly conserved protein from mycobacterial strains. However, no structural and functional information is associated with it. Thus, to obtain details about structure and function of this protein, we have utilized NMR spectroscopy. The recombinant MRA1997 was highly purified and its DNA binding mode was characterized. The tertiary structure of MRA1997 was modeled on the basis of our NMR chemical shift data combined with the webserver CS23D. The binding of MRA1997 with DNA was first monitored by electrophoresis mobility shift assays. The residues involved in DNA binding are identified using NMR chemical shift perturbation experiments. Based on our study, we suggest that MRA1997 interacts with DNA and may play an important role in Mycobacterium tuberculosis physiology. Keywords Mycobacterium tuberculosis, MRA1997, NMR, EMSA |
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