期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 93, 期 -, 页码 1147-1154出版社
ELSEVIER
DOI: 10.1016/j.ijbiomac.2016.09.087
关键词
Microtubule affinity-regulating kinase 4; UBA domain; Protein stability; Protein aggregation; ATPase activity; Protein folding
资金
- Council of Scientific and Industrial Research
- Department of Science and Technology (DST), Government of India [EMR/2015/002372]
- DST
Microtubule affinity regulating Kinase 4 (MARK4) belongs to the family of AMP-activated protein kinase. It phosphorylates microtubule associated proteins at specific sites (Serine in KXGS motifs) in the microtubule-binding repeats. In our previous studies, two constructs, namely, kinase domain with 59 N-terminal residues (residues 1-310) and only kinase domain (residues 59-310) of MARK4 show aggregation at physiological pH. However, these two constructs were stable at extremes of pH conditions. Now the question arises: how is MARK4 stable at physiological pH in-vivo? To answer this question, we have successfully cloned, expressed, and purified UBA-domain along with the kinase domain of MARK4 and performed spectroscopic measurements and activity assays. We observed a pronounced secondary and tertiary structure and ATPase activity in the MARK4 at physiological pH. In conclusion, UBA domain may be important to maintain the structure, stability and activity of MARK4 under physiological conditions. (C) 2016 Elsevier B.V. All rights reserved.
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