The N Terminus of ClpB from Thermus thermophilus Is Not Essential for the Chaperone Activity
作者： Philipp Beinker , Sandra Schlee , Yvonne Groemping , Ralf Seidel , Jochen Reinstein
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摘要: ClpB from Thermus thermophilus belongs to the Clp/Hsp100 protein family and reactivates aggregates in cooperation with DnaK chaperone system. The mechanism of reactivation interaction system remains unclear. possesses two nucleotide binding domains, which are essential for function show a complex allosteric behavior. role N-terminal domain that precedes first is largely unknown. We purified characterized an shortened variant (ClpBDeltaN; amino acids 140-854), remained active refolding assays three different substrate proteins. In addition truncation did not significantly change affinities, nucleotide-dependent oligomerization, behavior protein. contrast casein stimulation ATPase activity by kappa-casein were affected. These results suggest function, does influence nucleotides, involved formation intermolecular contacts. It contributes site ClpB, but other proteins do necessarily interact N terminus. This indicates substantial difference mode often used as model possibly more suitable
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