Biochemical coupling of the two nucleotide binding domains of ClpB: covalent linkage is not a prerequisite for chaperone activity

• Published in: The Journal of biological chemistry Vol. 280; no. 45; pp. 37965 - 37973
• Main Authors: Beinker, Philipp, Schlee, Sandra, Auvula, Rajeswari, Reinstein, Jochen
• Format: Journal Article
• Language: English
• Published: United States 11.11.2005
• Subjects: Adenosine Triphosphatases - metabolism; Bacterial Proteins - metabolism; Heat-Shock Proteins - metabolism; Molecular Chaperones - metabolism; Nucleotides - metabolism; Protein Structure, Tertiary; RNA, Bacterial - metabolism; RNA, Messenger - metabolism; Thermus thermophilus; Thermus thermophilus - metabolism

ClpB cooperates with the DnaK chaperone system in the reactivation of protein from aggregates and is a member of the ATPases associated with a variety of cellular activities (AAA+) protein family. The underlying disaggregation reaction is dependent on ATP hydrolysis at both AAA cassettes of ClpB but...