DNA-Segment-Facilitated Dissociation of Fis and NHP6A from DNA Detected via Single-Molecule Mechanical Response-Reference-Cited by-同舟云学术

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DNA-Segment-Facilitated Dissociation of Fis and NHP6A from DNA Detected via Single-Molecule Mechanical Response

Published:2015-09 Issue:19 Volume:427 Page:3123-3136
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Giuntoli Rebecca D.,Linzer Nora B.,Banigan Edward J.,Sing Charles E.,de la Cruz Monica Olvera,Graham John S.,Johnson Reid C.,Marko John F.

Funder

National Science Foundation

National Institutes of Health (NIH)

International Institute for Nanotechnology Postdoctoral Fellowship (C.E.S.)

NIH

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference48 articles.

1. Concentration-dependent exchange accelerates turnover of proteins bound to double-stranded DNA;Graham;Nucleic Acids Res.,2011

2. Multiple-binding-site mechanism explains concentration-dependent unbinding rates of DNA-binding proteins;Sing;Nucleic Acids Res.,2014

3. Stochastic ratchet mechanisms for replacement of proteins bound to DNA;Cocco;Phys. Rev. Lett.,2014

4. Direct substitution and assisted dissociation pathways for turning off transcription by a MerR-family metalloregulator;Joshi;Proc. Natl. Acad. Sci. U. S. A.,2012

5. Simultaneous single-molecule measurements of phage T7 replisome composition and function reveal the mechanism of polymerase exchange;Loparo;Proc. Natl. Acad. Sci. U. S. A.,2011

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