A New Small and Resilient Nucleic Acid-Binding Protein from Nanoarchaeum equitans

Area of Science:

• Biochemistry
• Molecular Biology
• Biotechnology

Background:

• Nucleic acid-binding proteins (NBPs) regulate gene expression in all organisms.
• DNA- and RNA-binding proteins (DRBPs) are a specific class of NBPs with emerging applications.
• The archaeal protein Neq150 from *Nanoarchaeum equitans* is investigated for its binding properties.

Purpose of the Study:

• To characterize the nucleic acid binding capabilities of the Neq150 protein.
• To assess the stability and potential applications of Neq150 in biotechnology.

Main Methods:

• Recombinant Neq150 protein was purified using Immobilized Metal Affinity Chromatography (IMAC).
• Electrophoretic Mobility Shift Assay (EMSA) was employed to evaluate Neq150's binding affinity to various nucleic acids.
• Thermostability was assessed by incubating the protein at 99°C for 3 hours.

Main Results:

• Neq150 was successfully purified and confirmed to bind to both DNA and RNA, classifying it as a DRBP.
• The protein demonstrated remarkable thermostability, remaining intact after prolonged exposure to high temperatures (99°C for 3 hours).
• Neq150 exhibited significant long-term stability under diverse experimental conditions.

Conclusions:

• Neq150 is a novel DRBP with robust stability, making it a promising candidate for biotechnological and molecular biology applications.
• Its properties suggest potential use as an auxiliary protein, similar to other characterized NBPs from *N. equitans*.
• Further research into Neq150 could lead to advancements in gene editing and drug development.