Journal article
The RadA Recombinase and Paralogs of the Hyperthermophilic Archaeon Sulfolobus solfataricus
Methods in enzymology, Vol.600, pp.255-284
2018
Handle:
https://hdl.handle.net/2376/104530
PMID: 29458762
Abstract
Repair of DNA double-strand breaks is a critical function shared by organisms in all three domains of life. The majority of mechanistic understanding of this process has come from characterization of bacterial and eukaryotic proteins, while significantly less is known about analogous activities in the third, archaeal domain. Despite the physical resemblance of archaea to bacteria, archaeal proteins involved in break repair are remarkably similar to those used by eukaryotes. Investigating the function of the archaeal version of these proteins is, in many cases, simpler than working with eukaryotic homologs owing to their robust nature and ease of purification. In this chapter, we describe methods for purification and activity analysis for the RadA recombinase and its paralogs from the hyperthermophilic acidophilic archaeon Sulfolobus solfataricus.
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Details
- Title
- The RadA Recombinase and Paralogs of the Hyperthermophilic Archaeon Sulfolobus solfataricus
- Creators
- Michael L Rolfsmeier - School of Molecular Biosciences, Washington State University, Pullman, WA, United StatesCynthia A Haseltine - School of Molecular Biosciences, Washington State University, Pullman, WA, United States. Electronic address: chaseltine@wsu.edu
- Publication Details
- Methods in enzymology, Vol.600, pp.255-284
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- United States
- Identifiers
- 99900546640401842
- Language
- English
- Resource Type
- Journal article