Structural and Functional Characterization of RecG Helicase under Dilute and Molecular Crowding Conditions
Joint Authors
Sugimoto, Naoki
Miyoshi, Daisuke
Saxena, Sarika
Nagatoishi, Satoru
Source
Issue
Vol. 2012, Issue 2012 (31 Dec. 2012), pp.1-8, 8 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2012-08-08
Country of Publication
Egypt
No. of Pages
8
Main Subjects
Abstract EN
In an ATP-dependent reaction, the Escherichia coli RecG helicase unwinds DNA junctions in vitro.
We present evidence of a unique protein conformational change in the RecG helicase from an α-helix to a β-strand upon an ATP binding under dilute conditions using circular dichroism (CD) spectroscopy.
In contrast, under molecular crowding conditions, the α-helical conformation was stable even upon an ATP binding.
These distinct conformational behaviors were observed to be independent of Na+ and Mg2+.
Interestingly, CD measurements demonstrated that the spectra of a frayed duplex decreased with increasing of the RecG concentration both under dilute and molecular crowding conditions in the presence of ATP, suggesting that RecG unwound the frayed duplex.
Our findings raise the possibility that the α-helix and β-strand forms of RecG are a preactive and an active structure with the helicase activity, respectively.
American Psychological Association (APA)
Saxena, Sarika& Nagatoishi, Satoru& Miyoshi, Daisuke& Sugimoto, Naoki. 2012. Structural and Functional Characterization of RecG Helicase under Dilute and Molecular Crowding Conditions. Journal of Nucleic Acids،Vol. 2012, no. 2012, pp.1-8.
https://search.emarefa.net/detail/BIM-468501
Modern Language Association (MLA)
Saxena, Sarika…[et al.]. Structural and Functional Characterization of RecG Helicase under Dilute and Molecular Crowding Conditions. Journal of Nucleic Acids No. 2012 (2012), pp.1-8.
https://search.emarefa.net/detail/BIM-468501
American Medical Association (AMA)
Saxena, Sarika& Nagatoishi, Satoru& Miyoshi, Daisuke& Sugimoto, Naoki. Structural and Functional Characterization of RecG Helicase under Dilute and Molecular Crowding Conditions. Journal of Nucleic Acids. 2012. Vol. 2012, no. 2012, pp.1-8.
https://search.emarefa.net/detail/BIM-468501
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-468501