Journal article
Switch-like control of helicase processivity by single-stranded DNA binding protein
eLife, Vol.10, e60515
03/19/2021
DOI: 10.7554/eLife.60515
PMCID: PMC7997660
PMID: 33739282
Abstract
Helicases utilize nucleotide triphosphate (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 such as single-stranded DNA binding proteins. Such encounters regulate helicase function, although the underlying mechanisms remain largely unknown.
Ferroplasma acidarmanus
xeroderma pigmentosum group D (XPD) helicase serves as a model for understanding the molecular mechanisms of superfamily 2B helicases, and its activity is enhanced by the cognate single-stranded DNA binding protein replication protein A 2 (RPA2). Here, 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. A point mutation at a regulatory DNA binding site on XPD similarly activates this switch. These findings provide new insights on mechanisms of helicase regulation by accessory proteins.
Details
- Title: Subtitle
- Switch-like control of helicase processivity by single-stranded DNA binding protein
- Creators
- Barbara Stekas - University of Illinois Urbana-ChampaignSteve Yeo - University of Illinois Urbana-ChampaignAlice Troitskaia - University of Illinois Urbana-ChampaignMasayoshi Honda - Roy J. and Lucille A. Carver College of MedicineSei Sho - Roy J. and Lucille A. Carver College of MedicineMaria Spies - Roy J. and Lucille A. Carver College of MedicineYann R Chemla - University of Illinois Urbana-Champaign
- Resource Type
- Journal article
- Publication Details
- eLife, Vol.10, e60515
- DOI
- 10.7554/eLife.60515
- PMID
- 33739282
- PMCID
- PMC7997660
- NLM abbreviation
- Elife
- ISSN
- 2050-084X
- eISSN
- 2050-084X
- Grant note
- DOI: 10.13039/100000002, name: National Institutes of Health, award: R01 GM120353; DOI: 10.13039/100000002, name: National Institutes of Health, award: R35 GM131704
- Language
- English
- Date published
- 03/19/2021
- Academic Unit
- Radiation Oncology; Biochemistry and Molecular Biology
- Record Identifier
- 9984293075802771
Metrics
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