Helicases in DNA Repair: From Molecular Mechanisms to Medical and Biotechnological Applications

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Genetics".

Deadline for manuscript submissions: 23 May 2026 | Viewed by 633

Special Issue Editor


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Guest Editor
Department of Biochemistry, University of California, 900 University Avenue, Riverside, CA 92521, USA
Interests: structural biology; protein X-ray; crystallography; DNA repair and recombination; bacteria–host interactions

Special Issue Information

Dear Colleagues,

The international journal Biomolecules (impact factor of 4.8; cite score of 9.4) invites submissions to a Special Issue focused on helicases in DNA repair.

Helicases are a huge group of enzymes that utilizes ATP hydrolysis to unwind nucleic acid duplexes and plays an essential role in almost all aspects of nucleic acid metabolism, such as replication, transcription, and repair. This Special Issue will focus on helicases in DNA repair, which itself is a diverse biological process with different pathways for repairing various DNA damage.  Defects in helicases and/or abnormal regulations of helicase expression or action have sever impacts on genome stability. Although helicases have been studied by many scientists worldwide since the middle of last century, new mechanisms of helicase action or even new helicase members continue to emerge. Accordingly, applications of helicases in emerging biotechnologies and medicine continue to grow.

We encourage researchers that are interested in helicases, their role, and/or action in DNA repair, as well as their potential medical or industrial applications, to submit relevant research articles to this Special Issue. In addition, review articles that cover the related research topics and provide concluding remarks will also be considered.

We look forward to your contributions.

Prof. Dr. Li Fan
Guest Editor

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Keywords

  • DNA unwinding
  • DNA damage response
  • damage verification
  • genetic disease
  • premature aging
  • cancer
  • chemotherapy
  • gene therapy

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Published Papers (1 paper)

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Review

29 pages, 5630 KB  
Review
Integrating Structural, Biochemical, and Cellular Perspectives on the TFIIH Helicases XPB and XPD
by Marco Bravo and Li Fan
Biomolecules 2026, 16(3), 435; https://doi.org/10.3390/biom16030435 - 13 Mar 2026
Viewed by 377
Abstract
Xeroderma pigmentosum group B (XPB/ERCC3) and group D (XPD/ERCC2) helicases are integral components of the transcription factor IIH (TFIIH) complex, coordinating DNA unwinding during transcription initiation and nucleotide excision repair (NER). XPB functions as an ATP-driven translocase that generates torsional strain to promote [...] Read more.
Xeroderma pigmentosum group B (XPB/ERCC3) and group D (XPD/ERCC2) helicases are integral components of the transcription factor IIH (TFIIH) complex, coordinating DNA unwinding during transcription initiation and nucleotide excision repair (NER). XPB functions as an ATP-driven translocase that generates torsional strain to promote promoter melting and DNA opening at lesion sites, whereas XPD acts as a 5′ to 3′ helicase responsible for lesion verification and extension of the repair bubble. Structural and biochemical studies have clarified how TFIIH subunits regulate these helicases—p52 and p8 modulate XPB’s translocation activity, while p44, p62, and MAT1 control XPD’s helicase function through conformational and compositional transitions within the complex. Beyond their canonical roles, XPB and XPD participate in diverse cellular pathways, including cell-cycle regulation and oxidative stress response, highlighting their involvement in maintaining genome integrity beyond repair and transcription. Mutations in either helicase lead to xeroderma pigmentosum (XP), trichothiodystrophy (TTD), or combined XP/Cockayne syndrome (XP/CS) phenotypes, emphasizing the essential role of TFIIH integrity for human health. Recent biochemical and pharmacological advances have further revealed the therapeutic relevance of these helicases—XPB as a target of small-molecule inhibitors such as triptolide, Minnelide, and spironolactone, and XPD as a potential modulator of cancer sensitivity to DNA-damaging treatments. Collectively, XPB and XPD exemplify the structural and functional versatility of TFIIH helicases across repair, transcription, and genome maintenance. Full article
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