Magnetic Resonance
Magnetic Resonance
MR
Articles | Volume 2, issue 1
Articles | Volume 2, issue 1
https://doi.org/10.5194/mr-2-375-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
Special issue:
https://doi.org/10.5194/mr-2-375-2021
© Author(s) 2021. This work is distributed under
the Creative Commons Attribution 4.0 License.
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

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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.
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