title: Avidity for Polypeptide Binding by Nucleotide-Bound Hsp104 Structures.
abstract: Recent Hsp104 structural studies have reported both planar and helical models of the hexameric structure. The conformation of Hsp104 monomers within the hexamer is affected by nucleotide ligation. After nucleotide-driven hexamer formation, Hsp104-catalyzed disruption of protein aggregates requires binding to the peptide substrate. Here, we examine the oligomeric state of Hsp104 and its peptide binding competency in the absence of nucleotide and in the presence of ADP, ATPγS, AMPPNP, or AMPPCP. Surprisingly, we found that only ATPγS facilitates avid peptide binding by Hsp104. We propose that the modulation between high- and low-peptide affinity states observed with these ATP analogues is an important component of the disaggregation mechanism of Hsp104.
authors.affiliation: Department of Chemistry, University of Alabama at Birmingham , Birmingham, Alabama 35294, United States.
authors.forename: Clarissa L
authors.initials: CL
authors.lastname: Weaver
authors.affiliation: Department of Chemistry, University of Alabama at Birmingham , Birmingham, Alabama 35294, United States.
authors.forename: Elizabeth C
authors.initials: EC
authors.lastname: Duran
authors.affiliation: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Korrie L
authors.initials: KL
authors.lastname: Mack
authors.affiliation: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: JiaBei
authors.initials: J
authors.lastname: Lin
authors.affiliation: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Meredith E
authors.initials: ME
authors.lastname: Jackrel
authors.affiliation: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: Elizabeth A
authors.initials: EA
authors.lastname: Sweeny
authors.affiliation: Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania , Philadelphia, Pennsylvania 19104, United States.
authors.forename: James
authors.initials: J
authors.lastname: Shorter
authors.affiliation: Department of Chemistry, University of Alabama at Birmingham , Birmingham, Alabama 35294, United States.
authors.forename: Aaron L
authors.identifier: 0000-0001-8636-5411
authors.initials: AL
authors.lastname: Lucius
mesh_terms: D000255:Adenosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism*; D011485:Protein Binding; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D006360:Heat-Shock Proteins; D010455:Peptides; D029701:Saccharomyces cerevisiae Proteins; C022571:adenosine 5'-O-(3-thiotriphosphate); D000255:Adenosine Triphosphate