Articles | Volume 2, issue 1
Research article
04 Jun 2021
Research article |  | 04 Jun 2021

Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone

Chih-Ting Huang, Yei-Chen Lai, Szu-Yun Chen, Meng-Ru Ho, Yun-Wei Chiang, and Shang-Te Danny Hsu


Interactive discussion

Status: closed

Comment types: AC – author | RC – referee | CC – community | EC – editor | CEC – chief editor | : Report abuse
  • RC1: 'Comment on mr-2021-9', Anonymous Referee #1, 11 Feb 2021
  • RC2: 'Comment on mr-2021-9', Anonymous Referee #2, 03 Mar 2021
  • RC3: 'Comment on mr-2021-9', Anonymous Referee #3, 03 Mar 2021

Peer review completion

AR: Author's response | RR: Referee report | ED: Editor decision
AR by Shang-Te Danny Hsu on behalf of the Authors (12 Apr 2021)  Author's response    Author's tracked changes    Manuscript
ED: Referee Nomination & Report Request started (21 Apr 2021) by Hashim Al-Hashimi
RR by Anonymous Referee #3 (02 May 2021)
ED: Publish subject to corrections (02 May 2021) by Hashim Al-Hashimi
Short summary
Trigger factor (TF) is a conserved bacterial molecular chaperone that exists in a monomer–dimer equilibrium in solution. It binds to the ribosome as a monomer to facilitate folding of nascent polypeptide chains. We showed that dimeric TF exhibits distinct domain dynamics and conformational polymorphism and that TF contains multiple substrate binding sites that are only accessible in its monomeric form. The equilibrium of TF in different oligomeric states may serve as a regulatory mechanism.