Using Single-Molecule Approaches To Study Archaeal DNA-Binding Protein Alba1

Biochemistry ◽  
2013 ◽  
Vol 52 (44) ◽  
pp. 7714-7722 ◽  
Author(s):  
Yen-Wen Lu ◽  
Tao Huang ◽  
Cheng-Ting Tsai ◽  
Yu-Yung Chang ◽  
Hung-Wen Li ◽  
...  
2018 ◽  
Vol 46 (21) ◽  
pp. 11287-11302 ◽  
Author(s):  
Parminder Kaur ◽  
Matthew J Longley ◽  
Hai Pan ◽  
Hong Wang ◽  
William C Copeland

2020 ◽  
Author(s):  
Barbara Stekas ◽  
Masayoshi Honda ◽  
Maria Spies ◽  
Yann R. Chemla

Helicases utilize the energy of NTP hydrolysis to translocate along single-stranded nucleic acids (NA) and unwind the duplex. In the cell, helicases function in the context of other NA-associated proteins which regulate helicase function. For example, single-stranded DNA binding proteins are known to enhance helicase activity, although the underlying mechanisms remain largely unknown. F. acidarmanus XPD helicase serves as a model for understanding the molecular mechanisms of Superfamily 2B helicases, and previous work has shown that its activity is enhanced by the cognate single-stranded DNA binding protein RPA2. Here, single-molecule optical trap measurements of the unwinding activity of a single XPD helicase in the presence of RPA2 reveal a mechanism in which XPD interconverts between two states with different processivities and transient RPA2 interactions stabilize the more processive state, activating a latent “processivity switch” in XPD. These findings provide new insights on mechanisms of helicase regulation by accessory proteins.


2010 ◽  
Vol 222 (03) ◽  
Author(s):  
S Degen ◽  
S Kuhfittig-Kulle ◽  
JH Schulte ◽  
F Westermann ◽  
A Schramm ◽  
...  

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