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DNA Helicases and DNA Motor Proteins pp 17–46Cite as

Structure and Mechanisms of SF1 DNA Helicases

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

Abstract

Superfamily I is a large and diverse group of monomeric and dimeric helicases defined by a set of conserved sequence motifs. Members of this class are involved in essential processes in both DNA and RNA metabolism in all organisms. In addition to conserved amino acid sequences, they also share a common structure containing two RecA-like motifs involved in ATP binding and hydrolysis and nucleic acid binding and unwinding. Unwinding is facilitated by a “pin” structure which serves to split the incoming duplex. This activity has been measured using both ensemble and single-molecule conditions. SF1 helicase activity is modulated through interactions with other proteins.

The online version of the original chapter can be found at http://dx.doi.org/10.1007/978-1-4614-5037-5_14

An erratum to this chapter can be found at http://dx.doi.org/10.1007/978-1-4614-5037-5_14

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Acknowledgements

Funding for this work was provided by NIH R01 GM098922 (K.D.R.).

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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, AR, USA

    Kevin D. Raney, Alicia K. Byrd & Suja Aarattuthodiyil

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  1. Kevin D. Raney
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  2. Alicia K. Byrd
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  3. Suja Aarattuthodiyil
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Correspondence to Kevin D. Raney .

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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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Raney, K.D., Byrd, A.K., Aarattuthodiyil, S. (2013). Structure and Mechanisms of SF1 DNA Helicases. 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_2

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