Results 31 to 40 of about 5,379 (199)

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

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

Protein Homeostasis in Amyotrophic Lateral Sclerosis: Therapeutic Opportunities?

Frontiers in Molecular Neuroscience, 2017
Protein homeostasis (proteostasis), the correct balance between production and degradation of proteins, is essential for the health and survival of cells.
Pamela J. Shaw, Kurt J. De Vos, Christopher P. Webster, Emma F. Smith   +3 more
doaj   +1 more source

Type I chaperonins: not all are created equal [PDF]

, 2002
Type I chaperonins play an essential role in the folding of newly translated and stress-denatured proteins in eubacteria, mitochondria and chloroplasts.
Nir Ben-Tal, Ben-Tal, Nir, Rachel E Bell, Azem, Abdussalam, Galit Levy-Rimler, Bell, Rachel E, Abdussalam Azem, Levy-Rimler, Galit   +7 more
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

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

Chaperonin Abundance Enhances Bacterial Fitness

Frontiers in Molecular Biosciences, 2021
The ability of chaperonins to buffer mutations that affect protein folding pathways suggests that their abundance should be evolutionarily advantageous. Here, we investigate the effect of chaperonin overproduction on cellular fitness in Escherichia coli.
C. M. Santosh Kumar, Kritika Chugh, Anirban Dutta, Vishnuvardhan Mahamkali, Tungadri Bose, Sharmila S. Mande, Shekhar C. Mande, Peter A. Lund   +7 more
doaj   +1 more source

Comparative genomic analysis of mollicutes with and without a chaperonin system. [PDF]

PLoS ONE, 2018
The GroE chaperonin system, which comprises GroEL and GroES, assists protein folding in vivo and in vitro. It is conserved in all prokaryotes except in most, but not all, members of the class of mollicutes.
Dominik Schwarz, Orit Adato, Amnon Horovitz, Ron Unger   +3 more
doaj   +1 more source