Exploring the impact of nucleic acids on protein stability in bacterial cell lysate

• Published in: Biochimica et biophysica acta. General subjects Vol. 1867; no. 10; p. 130445
• Main Authors: Ham, Soojeong, Lee, Changhan
• Format: Journal Article
• Language: English
• Published: Elsevier B.V 01.10.2023
• Subjects: Anti-aggregation activity; bacteria; Chaperone; DNA; electrostatic interactions; Nucleic acids; RNA; salt concentration; thermal stability; Nucleic acids; RNA; DNA; Chaperone; Anti-aggregation activity
• ISSN: 0304-4165; 1872-8006; 1872-8006
• DOI: 10.1016/j.bbagen.2023.130445

- Addition of salt enhanced thermal stability of model substrate proteins by reducing electrostatic repulsion between protein molecules. - However, the opposite effect was observed with bacterial cell lysate, indicating that certain molecules within the lysate could enhance protein stability via electrostatic interactions. - Such molecules present in cell lysate were found to be nucleic acids known to have a potent anti-aggregation activity toward proteins involving electrostatic interactions. - Nucleic acids showed chaperone activity in physiological salt concentration within cells and in buffer or medium commonly used in experiments. - The chaperone activity of nucleic acids should be taken into account when performing various in vitro assays using cell lysate or samples containing nucleic acids.