Version 1
: Received: 31 January 2024 / Approved: 1 February 2024 / Online: 1 February 2024 (11:15:54 CET)
How to cite:
Azam, S.; Anjum, R.S. Sequence Fingerprints in HerA Helicase: Implications for DNA Repair and Cancer. Preprints2024, 2024020044. https://doi.org/10.20944/preprints202402.0044.v1
Azam, S.; Anjum, R.S. Sequence Fingerprints in HerA Helicase: Implications for DNA Repair and Cancer. Preprints 2024, 2024020044. https://doi.org/10.20944/preprints202402.0044.v1
Azam, S.; Anjum, R.S. Sequence Fingerprints in HerA Helicase: Implications for DNA Repair and Cancer. Preprints2024, 2024020044. https://doi.org/10.20944/preprints202402.0044.v1
APA Style
Azam, S., & Anjum, R.S. (2024). Sequence Fingerprints in <em>HerA </em>Helicase: Implications for DNA Repair and Cancer. Preprints. https://doi.org/10.20944/preprints202402.0044.v1
Chicago/Turabian Style
Azam, S. and Rana Salman Anjum. 2024 "Sequence Fingerprints in <em>HerA </em>Helicase: Implications for DNA Repair and Cancer" Preprints. https://doi.org/10.20944/preprints202402.0044.v1
Abstract
In archaea, the interaction of HerA helicase and NurA nuclease is required for 3' end resection during DNA double-stranded break repair, and its disruption results in unfaithful DNA repair. Interactions transpire by the four conserved domains, including the N-terminal HAS domain (HerA-ATP synthase), which serves as a binding site for the exonuclease NurA. As a HerA hexamer between its two subunits, the conserved C-terminal brace extension functions as an adjacent brace. DBD serves as a location for DNA binding, which causes the DNA strands to be propelled into the HerA pocket to begin unwinding. The putative pore entrance is made up of four helix coils, which provide a suitable charged surface for guiding DNA into the pore. The crystal structure of the complex HerA-NurA allows for the identification of key residues for protein-protein interaction. This allows us to predict that most archaeal HerA orthologs will be able to interact with one another. Archaeal HerA is a homo-hexameric assembly featuring a DNA-binding domain that is conserved. It also features distinctive ATP and NurA binding domains. Following the structure and sequence conservation criteria, we find one HerA ortholog in Pyrobaculum calidifontis and multiple HerA paralogs, but the role of none is established yet.Interestingly, orthologous HerA is part of an Mre11-Rad50 gene neighborhood while paralogous HerA is not, which could be misleading. As a result, it sought to describe the criteria that may be used as a possible fingerprint for identifying orthologous genes, as well as the cloning procedures and tactics that would aid in the confirmation of the HerA helicase in P. calidifontis. Their confirmation is based on PCR cloning and characterization following HerA construct creation.
Keywords
Pyrobaculum calidifontis; Helicase; Nuclease; DNA binding domain; N-terminal HAS domain
Subject
Biology and Life Sciences, Biochemistry and Molecular Biology
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
