Jang, Min Su Song, Woo Chul Shin, Seung Won Park, Kyung Soo Kim, Jinseok Kim, Dong-Ik Kim, Byung Woo Um, Soong Ho 2024-01-20T06:31:28Z 2024-01-20T06:31:28Z 2021-09-05 2015-08-10 0168-1656 https://pubs.kist.re.kr/handle/201004/125130 With the advent of nanotechnology, new functional modules (e.g., nanomotors, nanoprobes) have become essential in several medical fields. Generally, mechanical modulators systems are the principal components of most cutting-edge technologies in modern biomedical applications. However, the in vivo use of motile probes has raised many concerns due to their low sensitivity and non-biocompatibility. As an alternative, biological enzymatic engines have received increased attention. In particular, ATPases, which belong to a class of motile enzymes that catalyze chemical metabolic reactions, have emerged as a promising motor due to their improved biocompatibility and performance. However, ATPases usually suffer from lower functional activity and are difficult to express recombinantly in bacteria relative to their conventional and synthetic competitors. Here, we report a novel functional modified ATPase with both a simple purification protocol and enhanced motile activity. For this mutant ATPase, a new bacterial subcloning method was established. The ATPase-encoding sequence was redesigned so that the mutant ATPase could be easily produced in an Escherichia coli system. The modified thermophilic F-1-ATPase (mTF(1)-ATPase) demonstrated 17.8 unit/mg ATPase activity. We propose that derivatives of our ATPase may enable the development of novel in vitro and in vivo synthetic medical diagnostics, as well as therapeutics. (C) 2015 Elsevier B.V. All rights reserved. English ELSEVIER SCIENCE BV THERMOPHILIC BACTERIUM EXPRESSION COMPLEX F1-ATPASE SUBUNITS SYNTHASE SURFACE CORE A novel multigene cloning method for the production of a motile ATPase Article 10.1016/j.jbiotec.2015.04.022 1 JOURNAL OF BIOTECHNOLOGY, v.207, pp.1 - 7 JOURNAL OF BIOTECHNOLOGY 207 1 7 scie scopus 000356450400001 2-s2.0-84929326295 Biotechnology & Applied Microbiology Biotechnology & Applied Microbiology Article THERMOPHILIC BACTERIUM EXPRESSION COMPLEX F1-ATPASE SUBUNITS SYNTHASE SURFACE CORE mTF(1)-ATPase Subcloning Multi-gene Self-ligation Membrane protein