ArticleProceedings of the National Academy of Sciences of the United States of America1997
Chaperonin filaments: the archaeal cytoskeleton?
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 101 citations in OpenAlex.
- Structural Stability Comparisons Between Natural and Engineered Group II Chaperonins: Are Crenarchaeal "Heat Shock" Proteins Also "pH Shock" Resistant?Microorganisms · 2024Article
- Article
- Chaperonins: Nanocarriers with Biotechnological Applications.Nanomaterials (Basel, Switzerland) · 2021Review
- Structural Determination of a Filamentous Chaperone to Fabricate Electronically Conductive Metalloprotein Nanowires.ACS nano · 2020Article
- NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase.BMC biology · 2016Article
- Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent.Scientific reports · 2014Article
- Human CCT4 and CCT5 chaperonin subunits expressed in Escherichia coli form biologically active homo-oligomers.The Journal of biological chemistry · 2013Article
- Article
- The impact of conformational fluctuations on self-assembly: cooperative aggregation of archaeal chaperonin proteins.Nano letters · 2009Article
- A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii.Protein science : a publication of the Protein Society · 2007Article
- Functional taxonomy of bacterial hyperstructures.Microbiology and molecular biology reviews : MMBR · 2007Review
- Proteomic analysis of acidic chaperones, and stress proteins in extreme halophile Halobacterium NRC-1: a comparative proteomic approach to study heat shock response.Proteome science · 2006Article
- Expression and biochemical characterization of two small heat shock proteins from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7.Protein science : a publication of the Protein Society · 2004Article
- Intracellular localization of a group II chaperonin indicates a membrane-related function.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- The eukaryote chaperonin CCT is a cold shock protein in Saccharomyces cerevisiae.Cell stress & chaperones · 2002Article
- Assembly of chaperonin complexes.Molecular biotechnology · 2001Review
- The complete genome of the crenarchaeon Sulfolobus solfataricus P2.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Stress genes and proteins in the archaea.Microbiology and molecular biology reviews : MMBR · 1999Review
- Acquired thermotolerance and temperature-induced protein accumulation in the extremely thermophilic bacterium Rhodothermus obamensis.Journal of bacteriology · 1998Article
- Immunolocalization of Hsp60 in Legionella pneumophila.Journal of bacteriology · 1998Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chaperonins are high molecular mass double-ring structures composed of 60-kDa protein subunits. In the hyperthermophilic archaeon Sulfolobus shibatae the two chaperonin proteins represent approximately 4% of its total protein and have a combined intracellular concentration of >30 mg/ml. At concentrations >/= 0.5 mg/ml purified chaperonins form filaments in the presence of Mg2+ and nucleotides. Filament formation requires nucleotide binding (not hydrolysis), and occurs at physiological temperatures in biologically relevant buffers, including a buffer made from cell extracts. These observations suggest that chaperonin filaments may exist in vivo and the estimated 4600 chaperonins per cell suggest that such filaments could form an extensive cytostructure. We observed filamentous structures in unfixed, uranyl-acetate-stained S. shibatae cells, which resemble the chaperonin filaments in size and appearance. ImmunoGold (Janssen) labeling using chaperonin antibodies indicated that many chaperonins are associated with insoluble cellular structures and these structures appear to be filamentous in some areas, although they could not be uranyl-acetate-stained. The existence of chaperonin filaments in vivo suggests a mechanism whereby their protein-folding activities can be regulated. More generally, the filaments themselves may play a cytoskeletal role in Archaea.
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