Insilico Structural and Functional Profiling of the HerA (Helicase) Enzyme in Pyrobaculum ferriducens

Authors

  • Sabiya Azam Department of Biotechnology, University of Central Punjab, Pakistan
  • Zeemal Seemab Amin 1Department of Biotechnology, University of Central Punjab, Pakistan 2School of Biochemistry, Minhaj University Lahore, Pakistan
  • Ummay Habiba 1Department of Biotechnology, University of Central Punjab, Pakistan 2School of Biochemistry, Minhaj University Lahore, Pakistan
  • Waqar Ahmed 1Department of Biotechnology, University of Central Punjab, Pakistan 2School of Biochemistry, Minhaj University Lahore, Pakistan
  • Saba Javaid 1Department of Biotechnology, University of Central Punjab, Pakistan 2School of Biochemistry, Minhaj University Lahore, Pakistan

DOI:

https://doi.org/10.63147/krjs.v5i1.235

Keywords:

DSB (double stranded break), HR (Homologous Recombination), ssDNA (single stranded DNA), HAS (HerA ATP Synthase), DBD (DNA binding domain)

Abstract

DNA double-strand breaks (DSBs) are significant DNA lesions that, if left unrepaired, compromise the integrity of the genome, while the role of DNA helicases in DNA unwinding during DNA repair processes cannot be overstated. This study aims to investigate the structural and functional role of the DNA helicase HerA in the repair of DNA double-strand breaks in the thermophilic archaeon Pyrobaculum ferrireducens using an insilico approach. Insilico studies help to understand the role of HerA in DNA double-strand break repair, including the binding site of the protein with its interacting partners, as well as the impact of point mutations on the function of the DNA helicase. The homology of the DNA helicase HerA with other DNA repair enzymes, as well as its structural homology with other DNA helicases, indicates that it plays a significant role in DNA double-strand break repair in the thermophilic archaeon Pyrobaculum ferrireducens, possibly as a result of evolutionary adaptations to survive in extreme environments under stress conditions. The results provide a computational framework for cross-species helicase research and validate HerA crucial role in DSB end resection for homologous recombination, reflecting evolutionary adaptations for extremophile survival. By addressing gaps in our understanding of archaeal DNA repair, synthetic biology for robust enzymes, and possibly eukaryotic repair defects associated with cancer, will get advanced. Through optimized commercial production of thermostable HerA for high-temperature industrial processes such as PCR, biofuel production, and diagnostics, it benefits biotechnology socially. Future prospects include directed evolution for improved variants, experimental validation, and applications in anti-cancer therapies that target repair helicases.

Author Biographies

  • Sabiya Azam, Department of Biotechnology, University of Central Punjab, Pakistan

    Lab-Engineer

    Department of Biochemistry and Biotechnology

  • Zeemal Seemab Amin, 1Department of Biotechnology, University of Central Punjab, Pakistan 2School of Biochemistry, Minhaj University Lahore, Pakistan

    Assistant Professor

    Department of Biochemistry

    Minhaj University of Lahore

  • Saba Javaid, 1Department of Biotechnology, University of Central Punjab, Pakistan 2School of Biochemistry, Minhaj University Lahore, Pakistan

    PhD scholar 

    Department of Biotechnology

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Published

31-03-2026

Issue

Vol. 5 No. 1 (2026): Kashmir Journal of Science

Section

Biological Sciences

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Copyright (c) 2026 Sabiya Azam, Zeemal Seemab Amin, Ummay Habiba, Waqar Ahmed, Saba Javaid

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This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.

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How to Cite

Insilico Structural and Functional Profiling of the HerA (Helicase) Enzyme in Pyrobaculum ferriducens. (2026). Kashmir Journal of Science, 5(1). https://doi.org/10.63147/krjs.v5i1.235