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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Field: Liquid-state NMR | Topic: Applications – biological macromolecules
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Cited articles

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Buskiewicz, I., Deuerling, E., Gu, S. Q., Jockel, J., Rodnina, M. V., Bukau, B., and Wintermeyer, W.: Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptor, P. Natl. Acad. Sci. USA, 101, 7902–7906,, 2004. 
Cabrita, L. D., Hsu, S.-T. D., Launay, H., Dobson, C. M., and Christodoulou, J.: Probing ribosome-nascent chain complexes produced in vivo by NMR spectroscopy, P. Natl. Acad. Sci. USA, 106, 22239–22244,, 2009. 
Cabrita, L. D., Cassaignau, A. M. E., Launay, H. M. M., Waudby, C. A., Wlodarski, T., Camilloni, C., Karyadi, M.-E., Robertson, A. L., Wang, X., Wentink, A. S., Goodsell, L. S., Woolhead, C. A., Vendruscolo, M., Dobson, C. M., snd Christodoulou, J.: A structural ensemble of a ribosome-nascent chain complex during cotranslational protein folding, Nat. Struct. Mol. Biol., 23, 278–285,, 2016. 
Chiang, Y. W., Borbat, P. P., and Freed, J. H.: The determination of pair distance distributions by pulsed ESR using Tikhonov regularization, J. Magn. Reson., 172, 279–295,, 2005a. 
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.