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A structural feature of Dda helicase which enhances displacement of streptavidin and trp repressor from DNA.
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.
Afiliación
  • Byrd AK; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Malone EG; Winthrop P. Rockefeller Cancer Institute, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Hazeslip L; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Zafar MK; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Harrison DK; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Thompson MD; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Gao J; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Perumal SK; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
  • Marecki JC; Department of Chemistry, The Pennsylvania State University, University Park, Pennsylvania, USA.
  • Raney KD; Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, Little Rock, Arkansas, USA.
Protein Sci ; 31(2): 407-421, 2022 02.
Article en En | MEDLINE | ID: mdl-34761452
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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Virales / Bacteriófago T4 / ADN Helicasas Tipo de estudio: Prognostic_studies Idioma: En Revista: Protein Sci Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Virales / Bacteriófago T4 / ADN Helicasas Tipo de estudio: Prognostic_studies Idioma: En Revista: Protein Sci Asunto de la revista: BIOQUIMICA Año: 2022 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos