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Roles for Helicases as ATP-Dependent Molecular Switches

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DNA Helicases and DNA Motor Proteins

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 767))

Abstract

On the basis of the familial name, a “helicase” might be expected to have an enzymatic activity that unwinds duplex polynucleotides to form single strands. A more encompassing taxonomy that captures alternative enzymatic roles has defined helicases as a sub-class of molecular motors that move directionally and processively along nucleic acids, the so-called “translocases”. However, even this definition may be limiting in capturing the full scope of helicase mechanism and activity. Discussed here is another, alternative view of helicases—as machines which couple NTP-binding and hydrolysis to changes in protein conformation to resolve stable nucleoprotein assembly states. This “molecular switch” role differs from the classical view of helicases as molecular motors in that only a single catalytic NTPase cycle may be involved. This is illustrated using results obtained with the DEAD-box family of RNA helicases and with a model bacterial system, the ATP-dependent Type III restriction-modification enzymes. Further examples are discussed and illustrate the wide-ranging examples of molecular switches in genome metabolism.

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Acknowledgements

I thank Ralf Seidel, Steve Halford, Dale Wigley, Mark Dillingham, Nigel Savery, Julia Toth, Fiona Diffin and Kara van Aelst for discussions about helicases and restriction enzymes and for experimental assistance.

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  1. School of Biochemistry, University of Bristol, Medical Sciences Building, Bristol, UK

    Mark D. Szczelkun

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  1. Mark D. Szczelkun
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Correspondence to Mark D. Szczelkun .

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  1. , Department of Biochemistry, University of Iowa Carver College of Med, Newton Rd. 51, Iowa City, 52242, Iowa, USA

    Maria Spies

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Szczelkun, M.D. (2013). Roles for Helicases as ATP-Dependent Molecular Switches. In: Spies, M. (eds) DNA Helicases and DNA Motor Proteins. Advances in Experimental Medicine and Biology, vol 767. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-5037-5_11

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