A structural feature of Dda helicase which enhances displacement of streptavidin and trp repressor from DNA. (22nd November 2021)

• Record Type: Journal Article
• Authors: Byrd, Alicia K.; Malone, Emory G.; Hazeslip, Lindsey; Zafar, Maroof Khan; Harrison, David K.; Thompson, Matthew D.; Gao, Jun; Perumal, Senthil K.; Marecki, John C.; Raney, Kevin D.
• Is Part Of: Protein science. Volume 31:Number 2(2022)
• Page Start: 407
• Page End: 421
• Publication Date: 2021-11-22
• Subjects: DNA unwinding -- helicase -- pre‐steady‐state kinetics -- protein displacement -- structure; Proteins -- Periodicals; 572.6
• DOI: 10.1002/pro.4232
• Languages: English
• ISSNs: 0961-8368

Abstract

Abstract: Helicases are molecular motors with many activities. They use the energy from ATP hydrolysis to unwind double‐stranded nucleic acids while translocating on the single‐stranded DNA. In addition to unwinding, many helicases are able to remove proteins from nucleic acids. Bacteriophage T4 Dda is able to displace a variety of DNA binding proteins and streptavidin bound to biotinylated oligonucleotides. We have identified a subdomain of Dda that when deleted, results in a protein variant that has nearly wild type activity for unwinding double‐stranded DNA but exhibits greatly reduced streptavidin displacement activity. Interestingly, this domain has little effect on displacement of either gp32 or BamHI bound to DNA but does affect displacement of trp repressor from DNA. With this variant, we have identified residues which enhance displacement of some proteins from DNA.