EMSA and Single-Molecule Force Spectroscopy Study of Interactions betweenBacillus subtilisSingle-Stranded DNA-Binding Protein and Single-Stranded DNA

Langmuir ◽  
2011 ◽  
Vol 27 (24) ◽  
pp. 15008-15015 ◽  
Author(s):  
Wei Zhang ◽  
Xiujuan Lü ◽  
Wenke Zhang ◽  
Jiacong Shen
Keyword(s):  
Dna Binding ◽  
Single Molecule ◽  
Binding Protein ◽  
Force Spectroscopy ◽  
Dna Binding Protein ◽  
Spectroscopy Study ◽  
Single Molecule Force Spectroscopy ◽  
Single Stranded Dna

scholarly journals Single-molecule DREEM imaging reveals DNA wrapping around human mitochondrial single-stranded DNA binding protein

2018 ◽  
Vol 46 (21) ◽  
pp. 11287-11302 ◽  
Author(s):  
Parminder Kaur ◽  
Matthew J Longley ◽  
Hai Pan ◽  
Hong Wang ◽  
William C Copeland
Keyword(s):  
Dna Binding ◽  
Single Molecule ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Dna Wrapping

scholarly journals Switch-like control of helicase processivity by single-stranded DNA binding protein

2020 ◽  
Author(s):  
Barbara Stekas ◽  
Masayoshi Honda ◽  
Maria Spies ◽  
Yann R. Chemla
Keyword(s):  
Dna Binding ◽  
Single Molecule ◽  
Molecular Mechanisms ◽  
Binding Protein ◽  
Optical Trap ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Associated Proteins ◽  
Underlying Mechanisms ◽  
Xpd Helicase

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.

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