ArticleProtein science : a publication of the Protein Society2007
A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 63 citations in OpenAlex.
- A Versatile Protein Scaffold Engineered for the Hierarchical Assembly of Robust and Highly Active Enzymes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- STORM Super-Resolution Visualization of Self-Assembled γPFD Chaperone Ultrastructures inNano letters · 2024Article
- Prefoldin 2 contributes to mitochondrial morphology and function.BMC biology · 2023Article
- Review
- Enhanced Production of SolubleJournal of microbiology and biotechnology · 2021Article
- Prefoldin Function in Cellular Protein Homeostasis and Human Diseases.Frontiers in cell and developmental biology · 2021Review
- Structural Determination of a Filamentous Chaperone to Fabricate Electronically Conductive Metalloprotein Nanowires.ACS nano · 2020Article
- The functions and mechanisms of prefoldin complex and prefoldin-subunits.Cell & bioscience · 2020Review
- Engineering bioorthogonal protein-polymer hybrid hydrogel as a functional protein immobilization platform.Chemical communications (Cambridge, England) · 2019Article
- Prefoldin, a jellyfish-like molecular chaperone: functional cooperation with a group II chaperonin and beyond.Biophysical reviews · 2018Review
- Geometrical assembly of ultrastable protein templates for nanomaterials.Nature communications · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Prefoldin is a molecular chaperone found in the domains eukarya and archaea that acts in conjunction with Group II chaperonin to correctly fold other nascent proteins. Previously, our group identified a putative single subunit of prefoldin, gamma PFD, that was up-regulated in response to heat stress in the hyperthermophilic archaeon Methanocaldococcus jannaschii. In order to characterize this protein, we subcloned and expressed it and the other two prefoldin subunits from M. jannaschii, alpha and beta PFD, into Eschericia coli and characterized the proteins. Whereas alpha and beta PFD readily assembled into the expected hexamer, gamma PFD would not assemble with either protein. Instead, gamma PFD forms long filaments of defined dimensions measuring 8.5 nm x 1.7-3.5 nm and lengths exceeding 1 microm. Filamentous gamma PFD acts as a molecular chaperone through in vitro assays, in a manner comparable to PFD. A possible molecular model for filament assembly is discussed.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.