Results 21 to 30 of about 8,317 (219)

CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin

Nature Communications, 2021
The mechanism by which chaperonins coordinate ATP utilization in their multiple subunits remains unclear. Here, the authors employ an approach that uses cryo-EM single particle analysis to track the number and distribution of nucleotides bound to each ...
Yanyan Zhao, Michael F. Schmid, Judith Frydman, Wah Chiu   +3 more
doaj   +1 more source

Functional divergence of chloroplast Cpn60α subunits during Arabidopsis embryo development. [PDF]

PLoS Genetics, 2017
Chaperonins are a class of molecular chaperones that assist in the folding and assembly of a wide range of substrates. In plants, chloroplast chaperonins are composed of two different types of subunits, Cpn60α and Cpn60β, and duplication of Cpn60α and ...
Xiaolong Ke, Wenxuan Zou, Yafang Ren, Zhiqin Wang, Jin Li, Xuan Wu, Jie Zhao   +6 more
doaj   +1 more source

Archaeal chaperonins

Frontiers in Bioscience, 2009
Chaperonins are ubiquitous and essential protein folding machines. They have a striking structure, with two rings of seven, eight, or nine protomers forming a "double doughnut" complex, with the cavity in each ring being the likely site for protein folding to take place. The group I chaperonins, found in bacteria and the organelles descended from them,
Andrew T, Large, Peter A, Lund
openaire   +2 more sources

A yeast two-hybrid screen reveals a strong interaction between the Legionella chaperonin Hsp60 and the host cell small heat shock protein Hsp10 [PDF]

, 2015
L. pneumophila is an intracellular bacterium that replicates inside a membrane-bound vacuole called Legionella-containing vacuole (LCV), where it plentifully liberates its HtpB chaperonin.
Nasrallah, Gheyath K.
core   +1 more source

Crystal structure of P. falciparum Cpn60 bound to ATP reveals an open dynamic conformation before substrate binding

Scientific Reports, 2021
Plasmodium falciparum harbors group 1 and group 2 chaperonin systems to mediate the folding of cellular proteins in different cellular locations. Two distinct group 1 chaperonins operate in the organelles of mitochondria and apicoplasts, while group 2 ...
Brian Nguyen, Rui Ma, Wai Kwan Tang, Dashuang Shi, Niraj H. Tolia   +4 more
doaj   +1 more source

Transcriptome profiling of grapevine seedless segregants during berry development reveals candidate genes associated with berry weight [PDF]

, 2016
Indexación: Web of Science; PubMedBackground Berry size is considered as one of the main selection criteria in table grape breeding programs. However, this is a quantitative and polygenic trait, and its genetic determination is still poorly understood ...
A Doligez, A Roberts, A Zamboni, AJ Bais, Alejandro Maass, Alex Di Genova, AM Almeida, AP Friend, Ariel Orellana, AS Negri, BG Coombe, BG Coombe, BG Coombe, BM Fischer, C Chen, C Conde, C Houel, C Pastore, C Pratt, C Sweetman, C Trapnell, CA Ledbetter, Claudia Muñoz-Espinoza, D Costenaro da Silva, D Lijavetzki, D Moreno, D Schenck, DH Lorenz, F Carrari, F Dyda, FG Silva da, FJ Pérez, G Fanizza, GR Cramer, I Debeaujon, J Correa, J Correa, J Guo, J Tello, J Xu, JA Cabezas, José Correa, JP Nitsch, K Chen, K Yang, KCH Amrine, L Bogrë, L Costantini, L Deluc, L Fernandez, M Barticevic, M Chakrabarti, M Fasoli, M González-Agüero, M Lu, M Rienth, M Salmaso, Mauricio González-Agüero, MB Ali, MC Palumbo, MJ Carmona, MJ Martínez-Esteso, MK Aradhya, N Mejía, N Mejía, N Schumann, N Wang, N Yokotani, NS Watson-Haigh, O Gudenschwager, O Jaillon, P Barba, P Langcake, P Neudecker, P Nicolas, Patricio Hinrichsen, R Core Team, R Ursem, Romina Silva, S Dal Santo, S Epskamp, S Guillaumie, S Lê, S Myles, S Taylor, S Zenoni, SBP Athauda, T Sekito, T Wei, X Chen, Z Du   +90 more
core   +3 more sources

Overexpression of a Prefoldin β subunit gene reduces biomass recalcitrance in the bioenergy crop Populus. [PDF]

, 2020
Prefoldin (PFD) is a group II chaperonin that is ubiquitously present in the eukaryotic kingdom. Six subunits (PFD1-6) form a jellyfish-like heterohexameric PFD complex and function in protein folding and cytoskeleton organization.
Barry, Kerrie, Bryan, Anthony C, Chen, Jin-Gui, Collins, Cassandra M, Ding, Jinhua, Engle, Nancy L, Gunter, Lee E, Jawdy, Sara S, Li, Mi, Lindquist, Erika A, Muchero, Wellington, Pu, Yunqiao, Rottmann, William, Schmutz, Jeremy, Singan, Vasanth, Tschaplinski, Timothy J, Tuskan, Gerald A, Winkeler, Kimberly A, Xie, Meng, Yang, Xiaohan, Zhang, Jin   +20 more
core   +1 more source

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES

Frontiers in Microbiology, 2017
Chaperonin GroEL (Cpn60) requires cofactor GroES (Cpn10) for protein refolding in bacteria that possess single groEL and groES genes in a bicistronic groESL operon.
Yue-zhong Li, Li Zhuo, Yan Wang, Yan Wang, Zheng Zhang, Jian Li, Xiao-Hua Zhang   +6 more
doaj   +1 more source

The ribosome modulates folding inside the ribosomal exit tunnel

Communications Biology, 2021
Wruck et al. investigate the folding of the small zinc-finger domain ADR1a inside and at the vestibule of the ribosomal tunnel, using optical tweezers, single-molecule FRET, and molecular dynamics simulations.
Florian Wruck, Pengfei Tian, Renuka Kudva, Robert B. Best, Gunnar von Heijne, Sander J. Tans, Alexandros Katranidis   +6 more
doaj   +1 more source

The Functional Differences between the GroEL Chaperonin of Escherichia coli and the HtpB Chaperonin of Legionella pneumophila Can Be Mapped to Specific Amino Acid Residues

Biomolecules, 2021
Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles.
Karla N. Valenzuela-Valderas, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduño   +3 more
doaj   +1 more source