Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation
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Motif III is one of the seven protein motifs that are characteristic of superfamily I helicases. To investigate its role in the helicase mechanism we have introduced a variety of mutations at three of the most conserved amino acid residues (Q254, W259 and R260). Biochemical characterisation of the resulting proteins shows that mutation of motif III affects both ATP hydrolysis and single-stranded DNA binding. We propose that amino acid residue Q254 acts as a gamma-phosphate sensor at the nucleotide binding pocket transmitting conformational changes to the DNA binding site, since the nature of the charge on this residue appears to control the degree of coupling between ATPase and helicase activities. Residues W259 and R260 both participate in direct DNA binding interactions that are critical for helicase activity.
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The AN935_03395 gene encodes ATP-dependent DNA helicase PcrA, and its mutation may lead to loss of protein function, with inability to hydrolyze ATP and make conformational changes essential for binding to ssDNA.
“The AN935_03395 gene encodes the ATP-dependent DNA helicase PcrA, a specific bacterial helicase that belongs to the UvrD/Rep helicase family with double activity, ssDNA translocation and duplex destabilization; its mutation may thus lead to a loss of protein function, with an inability to hydrolyze ATP and thus to make conformational changes essential for binding to ssDNA [95].”
From Profiling the resistome and virulome of Bacillus strains used for probiotic-based sanitation: a multicenter WGS analysis (2025) · cites this paper as [95]
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ATP binding leads to autophosphorylation of HSV-1 origin binding protein
Schildgen, O. (2016) · Molecular Genetics Microbiology and Virology · doi:10.3103/s0891416816030095
Structure and function of the human RecQ DNA helicases
Garcia, P. L. (2005) · Zurich Open Repository and Archive (University of Zurich) · doi:10.5167/uzh-34420
Faculty Opinions recommendation of Structural mechanisms of PriA-mediated DNA replication restart.
Eichman, B. F. (2014) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.718219229.793489208
UvrD-like helicase Hmi1 Has an ATP independent role in yeast mitochondrial DNA maintenance
Sillamaa, S., Piljukov, V., Vaask, I., Sedman, T., Jõers, P., & Sedman, J. (2023) · DNA repair · doi:10.1016/j.dnarep.2023.103582
- Authors
- Dillingham, M. S., Soultanas, P., & Wigley, D. B.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Wigley, D. B.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 1999-08-01
- Volume
- 27
- Issue
- 16
- Pages
- 3310-3317
- ISSN
- 0305-1048 (ISSN-L)
- 1362-4962
- PMC
- PMC148564
- OpenAlex
- W2128298547
- Cited by
- 94
- References
- 23
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 2 · 2021: 4 · 2020: 4 · 2018: 3 · 2016: 3 · 2015: 2 · 2014: 4 · 2013: 2 · 2012: 5
- FWCI
- 1.71
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nucleic Acids Research (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Explore Bristol Research (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- ATP hydrolysis, DNA strand separation, single-stranded DNA binding, nucleotide-binding pocket, DNA binding sites, helicase mechanism, site-directed mutagenesis
- MeSH terms
- Adenosine Triphosphatases, Adenosine Triphosphate, Bacterial Proteins, DNA Helicases, DNA, Single-Stranded, Hydrolysis, Mutagenesis, Site-Directed
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