Backbone chemical shift assignment and dynamics of the N-terminal domain of ClpB from Francisella tularensis type VI secretion system

Biomol NMR Assign. 2022 Apr;16(1):75-79. doi: 10.1007/s12104-021-10062-3. Epub 2022 Jan 5.

Abstract

The Hsp100 family member ClpB is a protein disaggregase which solubilizes and reactivates stress-induced protein aggregates in cooperation with the DnaK/Hsp70 chaperone system. In the pathogenic bacterium Francisella tularensis, ClpB is involved in type VI secretion system (T6SS) disassembly through depolymerization of the IglA-IglB sheath. This leads to recycling and reassembly of T6SS components and this process is essential for the virulence of the bacterium. Here we report the backbone chemical shift assignments and 15N relaxation-based backbone dynamics of the N-terminal substrate-binding domain of ClpB (1-156).

Keywords: 15N relaxation; ClpB chaperone; Francisella tularensis; NMR resonance assignment; Type VI secretion system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli Proteins* / metabolism
  • Francisella tularensis* / metabolism
  • HSP70 Heat-Shock Proteins / metabolism
  • Nuclear Magnetic Resonance, Biomolecular
  • Type VI Secretion Systems* / metabolism
  • Virulence

Substances

  • Escherichia coli Proteins
  • HSP70 Heat-Shock Proteins
  • Type VI Secretion Systems