A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii

Timothy A. Whitehead, Boonchai B. Boonyaratanakornkit, Volker Höllrigl, Douglas S. Clark

Research output: Contribution to journalArticle

  • 17 Citations

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, γ 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, α and β PFD, into Eschericia coli and characterized the proteins. Whereas α and β PFD readily assembled into the expected hexamer, γ PFD would not assemble with either protein. Instead, γ PFD forms long filaments of defined dimensions measuring 8.5 nm x 1.7-3.5 nm and lengths exceeding 1 μm. Filamentous γ 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. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)626-634
Number of pages9
JournalProtein Science
Volume16
Issue number4
DOIs
StatePublished - Apr 2007
Externally publishedYes

Profile

Methanocaldococcus
Molecular Chaperones
Oceans and Seas
Proteins
Archaea
Group II Chaperonins
Heat-Shock Response
Molecular Models
Eukaryota
In Vitro Techniques
Acromion
Anthralin
Beryllium
Addison Disease
Ports and harbors
Hot Temperature

Keywords

  • Heat-shock response
  • Molecular chaperones
  • Prefoldin
  • Protein filaments

ASJC Scopus subject areas

  • Biochemistry

Cite this

A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii. / Whitehead, Timothy A.; Boonyaratanakornkit, Boonchai B.; Höllrigl, Volker; Clark, Douglas S.

In: Protein Science, Vol. 16, No. 4, 04.2007, p. 626-634.

Research output: Contribution to journalArticle

Whitehead, Timothy A.; Boonyaratanakornkit, Boonchai B.; Höllrigl, Volker; Clark, Douglas S. / A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii.

In: Protein Science, Vol. 16, No. 4, 04.2007, p. 626-634.

Research output: Contribution to journalArticle

@article{777f61db17504df1ae216f953febcf98,
title = "A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii",
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, γ 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, α and β PFD, into Eschericia coli and characterized the proteins. Whereas α and β PFD readily assembled into the expected hexamer, γ PFD would not assemble with either protein. Instead, γ PFD forms long filaments of defined dimensions measuring 8.5 nm x 1.7-3.5 nm and lengths exceeding 1 μm. Filamentous γ 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. Published by Cold Spring Harbor Laboratory Press.",
keywords = "Heat-shock response, Molecular chaperones, Prefoldin, Protein filaments",
author = "Whitehead, {Timothy A.} and Boonyaratanakornkit, {Boonchai B.} and Volker Höllrigl and Clark, {Douglas S.}",
year = "2007",
month = "4",
doi = "10.1110/ps.062599907",
volume = "16",
pages = "626--634",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "4",

}

TY - JOUR

T1 - A filamentous molecular chaperone of the prefoldin family from the deep-sea hyperthermophile Methanocaldococcus jannaschii

AU - Whitehead,Timothy A.

AU - Boonyaratanakornkit,Boonchai B.

AU - Höllrigl,Volker

AU - Clark,Douglas S.

PY - 2007/4

Y1 - 2007/4

N2 - 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, γ 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, α and β PFD, into Eschericia coli and characterized the proteins. Whereas α and β PFD readily assembled into the expected hexamer, γ PFD would not assemble with either protein. Instead, γ PFD forms long filaments of defined dimensions measuring 8.5 nm x 1.7-3.5 nm and lengths exceeding 1 μm. Filamentous γ 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. Published by Cold Spring Harbor Laboratory Press.

AB - 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, γ 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, α and β PFD, into Eschericia coli and characterized the proteins. Whereas α and β PFD readily assembled into the expected hexamer, γ PFD would not assemble with either protein. Instead, γ PFD forms long filaments of defined dimensions measuring 8.5 nm x 1.7-3.5 nm and lengths exceeding 1 μm. Filamentous γ 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. Published by Cold Spring Harbor Laboratory Press.

KW - Heat-shock response

KW - Molecular chaperones

KW - Prefoldin

KW - Protein filaments

UR - http://www.scopus.com/inward/record.url?scp=33947720464&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33947720464&partnerID=8YFLogxK

U2 - 10.1110/ps.062599907

DO - 10.1110/ps.062599907

M3 - Article

VL - 16

SP - 626

EP - 634

JO - Protein Science

T2 - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 4

ER -