Cryo-EM structure of bovine chaperonin TRiC/CCT in open conformation-Reference-Cited by-同舟云学术

Cryo-EM structure of bovine chaperonin TRiC/CCT in open conformation

Published:2023-12-21 Issue:№3s, 2023 Volume:78 Page:40-46
ISSN:0137-0952
Container-title:Vestnik Moskovskogo universiteta. Seria 16. Biologia
language:ru
Short-container-title:Vestn. Mosk. Univ. Ser. 16. Biol.

Author:

Stanishneva-Konovalova T.B.¹^ORCID,Pichkur E.B.²,Kudryavtseva S.S.³,Yaroshevich I.A.¹,Semenov A.N.¹,Maksimov E.G.¹,Moiseenko A.V.¹,Volokh O.I.¹,Muronetz V.I.³

Affiliation:

1. Lomonosov Moscow State University

2. National Research Centre “Kurchatov institute

3. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University

Abstract

In this work, conditions were selected for obtaining a sample of eukaryotic chaperonin TRiC suitable for studying by cryo-electron microscopy. Using the method of differential scanning (time-resolved) fluorimetry, the temperature stability of protein samples at different concentrations of salt and glycerol was compared, and then the selected conditions were used to prepare the sample for microscopy. As a result, the structure of bovine TRiC in an open conformation was obtained at 4.42 Å resolution.

Funder

Russian Science Foundation

Publisher

Moscow University Press

Reference38 articles.

1. Gestaut D., Limatola A., Joachimiak L., Frydman J. The ATP-powered gymnastics of TRiC/CCT: an asymmetric protein folding machine with a symmetric origin story. Curr. Opin. Struct. Biol. 2019;55:50–58.

2. Yam A.Y., Xia Y., Lin H.T.J., Burlingame A., Gerstein M., Program B. Defining the TRiC/CCT interactome links chaperonin function to stabilization of newly-made proteins with complex topologies. Nat. Struct. Mol. Biol. 2008;15(12):1255–1262.

3. Bigotti M.G., Clarke A.R. Chaperonins: The hunt for the Group II mechanism. Arch. Biochem. Biophys. 2008;474(2):331–339.

4. Spiess C., Meyer A.S., Reissmann S., Frydman J. Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets. Trends Cell Biol. 2004;14(11):598–604.

5. Skjærven L., Cuellar J., Martinez A., Valpuesta J.M. Dynamics, flexibility, and allostery in molecular chaperonins. FEBS Lett. 2015;589(19):2522–2532.