title: Specificity of DnaK-peptide binding.
abstract: The sequence specificity of DnaK substrate binding has been studied using a peptide display library. Based on the amino acid patterns that appeared in this selection, short peptides were synthesized for direct measurements of DnaK affinity. The results show that peptides enriched in internal hydrophobic residues are preferential DnaK substrates, and negatively charged peptides have poor affinity. The isolated C-terminal domain of DnaK binds peptides. Peptide dissociation studies indicate that bound peptides are released from the C-terminal fragment and from DnaK at identical rates. ATP stimulates peptide dissociation from DnaK but not from the C-terminal fragment.
authors.affiliation: Institute of Cancer Research, College of Physicians and Surgeons, Columbia University, New York, NY 10032.
authors.forename: A
authors.initials: A
authors.lastname: Gragerov
authors.forename: L
authors.initials: L
authors.lastname: Zeng
authors.forename: X
authors.initials: X
authors.lastname: Zhao
authors.forename: W
authors.initials: W
authors.lastname: Burkholder
authors.forename: M E
authors.initials: ME
authors.lastname: Gottesman
mesh_terms: D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism; D001483:Base Sequence; D001667:Binding, Competitive; D017931:DNA Primers / Q000737:chemistry; D004926:Escherichia coli; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D017931:DNA Primers; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D010455:Peptides; C063842:dnaK protein, E coli