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Journal articles on the topic 'Eukaryotic prefoldin'

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Author: Grafiati

Published: 10 December 2022

Last updated: 28 January 2023

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1

Morita, Kento, Yohei Yamamoto, Ayaka Hori, Tomohiro Obata, Yuko Uno, Kyosuke Shinohara, Keiichi Noguchi, et al. "Expression, Functional Characterization, and Preliminary Crystallization of the Cochaperone Prefoldin from the Thermophilic Fungus Chaetomium thermophilum." International Journal of Molecular Sciences 19, no. 8 (August 19, 2018): 2452. http://dx.doi.org/10.3390/ijms19082452.

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Prefoldin is a hexameric molecular chaperone found in the cytosol of archaea and eukaryotes. Its hexameric complex is built from two related classes of subunits, and has the appearance of a jellyfish: Its body consists of a double β-barrel assembly with six long tentacle-like coiled coils protruding from it. Using the tentacles, prefoldin captures an unfolded protein substrate and transfers it to a group II chaperonin. Based on structural information from archaeal prefoldins, mechanisms of substrate recognition and prefoldin-chaperonin cooperation have been investigated. In contrast, the structure and mechanisms of eukaryotic prefoldins remain unknown. In this study, we succeeded in obtaining recombinant prefoldin from a thermophilic fungus, Chaetomium thermophilum (CtPFD). The recombinant CtPFD could not protect citrate synthase from thermal aggregation. However, CtPFD formed a complex with actin from chicken muscle and tubulin from porcine brain, suggesting substrate specificity. We succeeded in observing the complex formation of CtPFD and the group II chaperonin of C. thermophilum (CtCCT) by atomic force microscopy and electron microscopy. These interaction kinetics were analyzed by surface plasmon resonance using Biacore. Finally, we have shown the transfer of actin from CtPFD to CtCCT. The study of the folding pathway formed by CtPFD and CtCCT should provide important information on mechanisms of the eukaryotic prefoldin–chaperonin system.

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2

Knowlton, Jonathan J., Daniel Gestaut, Boxue Ma, Gwen Taylor, Alpay Burak Seven, Alexander Leitner, Gregory J. Wilson, et al. "Structural and functional dissection of reovirus capsid folding and assembly by the prefoldin-TRiC/CCT chaperone network." Proceedings of the National Academy of Sciences 118, no. 11 (March 8, 2021): e2018127118. http://dx.doi.org/10.1073/pnas.2018127118.

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Intracellular protein homeostasis is maintained by a network of chaperones that function to fold proteins into their native conformation. The eukaryotic TRiC chaperonin (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1) facilitates folding of a subset of proteins with folding constraints such as complex topologies. To better understand the mechanism of TRiC folding, we investigated the biogenesis of an obligate TRiC substrate, the reovirus σ3 capsid protein. We discovered that the σ3 protein interacts with a network of chaperones, including TRiC and prefoldin. Using a combination of cryoelectron microscopy, cross-linking mass spectrometry, and biochemical approaches, we establish functions for TRiC and prefoldin in folding σ3 and promoting its assembly into higher-order oligomers. These studies illuminate the molecular dynamics of σ3 folding and establish a biological function for TRiC in virus assembly. In addition, our findings provide structural and functional insight into the mechanism by which TRiC and prefoldin participate in the assembly of protein complexes.

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3

Simons, C. Torrey, An Staes, Heidi Rommelaere, Christophe Ampe, Sally A. Lewis, and Nicholas J. Cowan. "Selective Contribution of Eukaryotic Prefoldin Subunits to Actin and Tubulin Binding." Journal of Biological Chemistry 279, no. 6 (November 22, 2003): 4196–203. http://dx.doi.org/10.1074/jbc.m306053200.

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4

Leroux, M. R. "MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin." EMBO Journal 18, no. 23 (December 1, 1999): 6730–43. http://dx.doi.org/10.1093/emboj/18.23.6730.

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5

Aikawa, Yoshiki, Hiroshi Kida, Yuichi Nishitani, and Kunio Miki. "Expression, purification, crystallization and X-ray diffraction studies of the molecular chaperone prefoldin fromHomo sapiens." Acta Crystallographica Section F Structural Biology Communications 71, no. 9 (August 25, 2015): 1189–93. http://dx.doi.org/10.1107/s2053230x15013990.

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Proper protein folding is an essential process for all organisms. Prefoldin (PFD) is a molecular chaperone that assists protein folding by delivering non-native proteins to group II chaperonin. A heterohexamer of eukaryotic PFD has been shown to specifically recognize and deliver non-native actin and tubulin to chaperonin-containing TCP-1 (CCT), but the mechanism of specific recognition is still unclear. To determine its crystal structure, recombinant human PFD was reconstituted, purified and crystallized. X-ray diffraction data were collected to 4.7 Å resolution. The crystals belonged to space groupP21212, with unit-cell parametersa= 123.2,b= 152.4,c= 105.9 Å.

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6

Large, Andrew T., Martin D. Goldberg, and Peter A. Lund. "Chaperones and protein folding in the archaea." Biochemical Society Transactions 37, no. 1 (January 20, 2009): 46–51. http://dx.doi.org/10.1042/bst0370046.

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A survey of archaeal genomes for the presence of homologues of bacterial and eukaryotic chaperones reveals several interesting features. All archaea contain chaperonins, also known as Hsp60s (where Hsp is heat-shock protein). These are more similar to the type II chaperonins found in the eukaryotic cytosol than to the type I chaperonins found in bacteria, mitochondria and chloroplasts, although some archaea also contain type I chaperonin homologues, presumably acquired by horizontal gene transfer. Most archaea contain several genes for these proteins. Our studies on the type II chaperonins of the genetically tractable archaeon Haloferax volcanii have shown that only one of the three genes has to be present for the organisms to grow, but that there is some evidence for functional specialization between the different chaperonin proteins. All archaea also possess genes for prefoldin proteins and for small heat-shock proteins, but they generally lack genes for Hsp90 and Hsp100 homologues. Genes for Hsp70 (DnaK) and Hsp40 (DnaJ) homologues are only found in a subset of archaea. Thus chaperone-assisted protein folding in archaea is likely to display some unique features when compared with that in eukaryotes and bacteria, and there may be important differences in the process between euryarchaea and crenarchaea.

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7

Martínez-Fernández, Verónica, and Francisco Navarro. "Rpb5, a subunit shared by eukaryotic RNA polymerases, cooperates with prefoldin-like Bud27/URI." AIMS Genetics 5, no. 1 (2018): 63–74. http://dx.doi.org/10.3934/genet.2018.1.63.

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8

Kabir, M. Anaul, Wasim Uddin, Aswathy Narayanan, Praveen Kumar Reddy, M. Aman Jairajpuri, Fred Sherman, and Zulfiqar Ahmad. "Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding." Journal of Amino Acids 2011 (July 2, 2011): 1–16. http://dx.doi.org/10.4061/2011/843206.

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Molecular chaperones are a class of proteins responsible for proper folding of a large number of polypeptides in both prokaryotic and eukaryotic cells. Newly synthesized polypeptides are prone to nonspecific interactions, and many of them make toxic aggregates in absence of chaperones. The eukaryotic chaperonin CCT is a large, multisubunit, cylindrical structure having two identical rings stacked back to back. Each ring is composed of eight different but similar subunits and each subunit has three distinct domains. CCT assists folding of actin, tubulin, and numerous other cellular proteins in an ATP-dependent manner. The catalytic cooperativity of ATP binding/hydrolysis in CCT occurs in a sequential manner different from concerted cooperativity as shown for GroEL. Unlike GroEL, CCT does not have GroES-like cofactor, rather it has a built-in lid structure responsible for closing the central cavity. The CCT complex recognizes its substrates through diverse mechanisms involving hydrophobic or electrostatic interactions. Upstream factors like Hsp70 and Hsp90 also work in a concerted manner to transfer the substrate to CCT. Moreover, prefoldin, phosducin-like proteins, and Bag3 protein interact with CCT and modulate its function for the fine-tuning of protein folding process. Any misregulation of protein folding process leads to the formation of misfolded proteins or toxic aggregates which are linked to multiple pathological disorders.

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9

Martin-Benito, J. "Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT." EMBO Journal 21, no. 23 (December 1, 2002): 6377–86. http://dx.doi.org/10.1093/emboj/cdf640.

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10

Martín-Benito, Jaime, Juan Gómez-Reino, Peter C. Stirling, Victor F. Lundin, Paulino Gómez-Puertas, Jasminka Boskovic, Pablo Chacón, et al. "Divergent Substrate-Binding Mechanisms Reveal an Evolutionary Specialization of Eukaryotic Prefoldin Compared to Its Archaeal Counterpart." Structure 15, no. 1 (January 2007): 101–10. http://dx.doi.org/10.1016/j.str.2006.11.006.

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11

Mirón-García, María Carmen, Ana Isabel Garrido-Godino, Varinia García-Molinero, Francisco Hernández-Torres, Susana Rodríguez-Navarro, and Francisco Navarro. "The Prefoldin Bud27 Mediates the Assembly of the Eukaryotic RNA Polymerases in an Rpb5-Dependent Manner." PLoS Genetics 9, no. 2 (February 14, 2013): e1003297. http://dx.doi.org/10.1371/journal.pgen.1003297.

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12

Millán-Zambrano, Gonzalo, and Sebastián Chávez. "Nuclear functions of prefoldin." Open Biology 4, no. 7 (July 2014): 140085. http://dx.doi.org/10.1098/rsob.140085.

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Prefoldin is a cochaperone, present in all eukaryotes, that cooperates with the chaperonin CCT. It is known mainly for its functional relevance in the cytoplasmic folding of actin and tubulin monomers during cytoskeleton assembly. However, both canonical and prefoldin-like subunits of this heterohexameric complex have also been found in the nucleus, and are functionally connected with nuclear processes in yeast and metazoa. Plant prefoldin has also been detected in the nucleus and physically associated with a gene regulator. In this review, we summarize the information available on the involvement of prefoldin in nuclear phenomena, place special emphasis on gene transcription, and discuss the possibility of a global coordination between gene regulation and cytoplasmic dynamics mediated by prefoldin.

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13

Huen, Jennifer, Yoshito Kakihara, Francisca Ugwu, Kevin L. Y. Cheung, Joaquin Ortega, and Walid A. Houry. "Rvb1–Rvb2: essential ATP-dependent helicases for critical complexesThis paper is one of a selection of papers published in this special issue entitled 8th International Conference on AAA Proteins and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 88, no. 1 (February 2010): 29–40. http://dx.doi.org/10.1139/o09-122.

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Rvb1 and Rvb2 are highly conserved, essential AAA+ helicases found in a wide range of eukaryotes. The versatility of these helicases and their central role in the biology of the cell is evident from their involvement in a wide array of critical cellular complexes. Rvb1 and Rvb2 are components of the chromatin-remodeling complexes INO80, Swr-C, and BAF. They are also members of the histone acetyltransferase Tip60 complex, and the recently identified R2TP complex present in Saccharomyces cerevisiae and Homo sapiens; a complex that is involved in small nucleolar ribonucleoprotein (snoRNP) assembly. Furthermore, in humans, Rvb1 and Rvb2 have been identified in the URI prefoldin-like complex. In Drosophila, the Polycomb Repressive complex 1 contains Rvb2, but not Rvb1, and the Brahma complex contains Rvb1 and not Rvb2. Both of these complexes are involved in the regulation of growth and development genes in Drosophila. Rvbs are therefore crucial factors in various cellular processes. Their importance in chromatin remodeling, transcription regulation, DNA damage repair, telomerase assembly, mitotic spindle formation, and snoRNP biogenesis is discussed in this review.

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14

Tahmaz, Ismail, Somayeh Shahmoradi Ghahe, and Ulrike Topf. "Prefoldin Function in Cellular Protein Homeostasis and Human Diseases." Frontiers in Cell and Developmental Biology 9 (January 17, 2022). http://dx.doi.org/10.3389/fcell.2021.816214.

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Cellular functions are largely performed by proteins. Defects in the production, folding, or removal of proteins from the cell lead to perturbations in cellular functions that can result in pathological conditions for the organism. In cells, molecular chaperones are part of a network of surveillance mechanisms that maintains a functional proteome. Chaperones are involved in the folding of newly synthesized polypeptides and assist in refolding misfolded proteins and guiding proteins for degradation. The present review focuses on the molecular co-chaperone prefoldin. Its canonical function in eukaryotes involves the transfer of newly synthesized polypeptides of cytoskeletal proteins to the tailless complex polypeptide 1 ring complex (TRiC/CCT) chaperonin which assists folding of the polypeptide chain in an energy-dependent manner. The canonical function of prefoldin is well established, but recent research suggests its broader function in the maintenance of protein homeostasis under physiological and pathological conditions. Interestingly, non-canonical functions were identified for the prefoldin complex and also for its individual subunits. We discuss the latest findings on the prefoldin complex and its subunits in the regulation of transcription and proteasome-dependent protein degradation and its role in neurological diseases, cancer, viral infections and rare anomalies.

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15

Kumar, Vikash, Ankita Behl, Rumaisha Shoaib, Mohammad Abid, Maxim Shevtsov, and Shailja Singh. "Comparative structural insight into prefoldin subunints of archaea and eukaryotes with special emphasis on unexplored prefoldin of Plasmodium falciparum." Journal of Biomolecular Structure and Dynamics, December 4, 2020, 1–15. http://dx.doi.org/10.1080/07391102.2020.1850527.

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16

Blanco-Touriñán, Noel, David Esteve-Bruna, Antonio Serrano-Mislata, Rosa María Esquinas-Ariza, Francesca Resentini, Javier Forment, Cristian Carrasco-López, et al. "A genetic approach reveals different modes of action of prefoldins." Plant Physiology, July 23, 2021. http://dx.doi.org/10.1093/plphys/kiab348.

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Abstract The prefoldin complex (PFDc) was identified in humans as a co-chaperone of the cytosolic chaperonin T-COMPLEX PROTEIN RING COMPLEX (TRiC)/CHAPERONIN CONTAINING TCP-1 (CCT). PFDc is conserved in eukaryotes and is composed of subunits PFD1–6, and PFDc-TRiC/CCT folds actin and tubulins. PFDs also participate in a wide range of cellular processes, both in the cytoplasm and in the nucleus, and their malfunction causes developmental alterations and disease in animals and altered growth and environmental responses in yeast and plants. Genetic analyses in yeast indicate that not all of their functions require the canonical complex. The lack of systematic genetic analyses in plants and animals, however, makes it difficult to discern whether PFDs participate in a process as the canonical complex or in alternative configurations, which is necessary to understand their mode of action. To tackle this question, and on the premise that the canonical complex cannot be formed if one subunit is missing, we generated an Arabidopsis (Arabidopsis thaliana) mutant deficient in the six PFDs and compared various growth and environmental responses with those of the individual mutants. In this way, we demonstrate that the PFDc is required for seed germination, to delay flowering, or to respond to high salt stress or low temperature, whereas at least two PFDs redundantly attenuate the response to osmotic stress. A coexpression analysis of differentially expressed genes in the sextuple mutant identified several transcription factors, including ABA INSENSITIVE 5 (ABI5) and PHYTOCHROME-INTERACTING FACTOR 4, acting downstream of PFDs. Furthermore, the transcriptomic analysis allowed assigning additional roles for PFDs, for instance, in response to higher temperature.

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