A novel multigene cloning method for the production of a motile ATPase

Title
A novel multigene cloning method for the production of a motile ATPase
Authors
김진석장민수송우철신승원박경수김동익김병우엄숭호
Keywords
mTF1-ATPase; Subcloning; Multi-gene; Self-ligation; Membrane protein
Issue Date
2015-08
Publisher
Journal of biotechnology
Citation
VOL 207-7
Abstract
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.
URI
http://pubs.kist.re.kr/handle/201004/69262
ISSN
0168-1656
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KIST Publication > Article
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