Evidence map›Paper›PMID 26787517›Full record

ArticleNature communications2016

Protein unfolding as a switch from self-recognition to high-affinity client binding.

Bastian Groitl, Scott Horowitz, Karl A T Makepeace, Evgeniy V Petrotchenko, Christoph H Borchers, Dana Reichmann, James C A Bardwell, Ursula Jakob

Abstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

23 citing papers in PubMed.

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  16. Article
  17. Mechanical properties of BiP protein determined by nano-rheology.Protein science : a publication of the Protein Society · 2018
    Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Bastian GroitlDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N-University Avenue, Ann Arbor, Michigan 48109-1048, USA.
Scott HorowitzDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N-University Avenue, Ann Arbor, Michigan 48109-1048, USA.
Karl A T MakepeaceDepartment of Biochemistry and Microbiology, Genome BC Proteomics Centre, University of Victoria, 4464 Markham Street #3101, Victoria, British Columbia, Canada V8Z5N3.
Evgeniy V PetrotchenkoDepartment of Biochemistry and Microbiology, Genome BC Proteomics Centre, University of Victoria, 4464 Markham Street #3101, Victoria, British Columbia, Canada V8Z5N3.
Christoph H BorchersDepartment of Biochemistry and Microbiology, Genome BC Proteomics Centre, University of Victoria, 4464 Markham Street #3101, Victoria, British Columbia, Canada V8Z5N3.
Dana ReichmannDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N-University Avenue, Ann Arbor, Michigan 48109-1048, USA.
James C A BardwellDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N-University Avenue, Ann Arbor, Michigan 48109-1048, USA.
Ursula JakobDepartment of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N-University Avenue, Ann Arbor, Michigan 48109-1048, USA.

Funding

Functional Analysis of the Intrinsically Disordered Chaperone Hsp33R01GM065318 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2003 to 2015
$3.9M
Mechanism of an Acid Activated ChaperoneR01GM102829 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BARDWELL, JAMES, JAKOB, URSULA H. · 2013 to 2016
$1.8M
FUNCTIONAL ANALYSIS OF A PROTEIN FOLDING CATALYSTR01GM057039 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BARDWELL, JAMES · 1998 to 2006
$1.7M
Howard Hughes Medical InstituteNIGMS NIH HHS GM065318NIGMS NIH HHS R01 GM057039NIGMS NIH HHS R01 GM065318NIGMS NIH HHS R01 GM102829
6 · The paper itself

Abstract

Stress-specific activation of the chaperone Hsp33 requires the unfolding of a central linker region. This activation mechanism suggests an intriguing functional relationship between the chaperone's own partial unfolding and its ability to bind other partially folded client proteins. However, identifying where Hsp33 binds its clients has remained a major gap in our understanding of Hsp33's working mechanism. By using site-specific Fluorine-19 nuclear magnetic resonance experiments guided by in vivo crosslinking studies, we now reveal that the partial unfolding of Hsp33's linker region facilitates client binding to an amphipathic docking surface on Hsp33. Furthermore, our results provide experimental evidence for the direct involvement of conditionally disordered regions in unfolded protein binding. The observed structural similarities between Hsp33's own metastable linker region and client proteins present a possible model for how Hsp33 uses protein unfolding as a switch from self-recognition to high-affinity client binding.

Indexed as

Escherichia coli ProteinsFluorine-19 Magnetic Resonance ImagingHeat-Shock ProteinsMolecular ChaperonesPeptidesProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryProtein UnfoldingEscherichia coli ProteinsHeat-Shock ProteinsHSP33 protein, E coliMolecular ChaperonesPeptides

Identifiers

PMID26787517
PMCPMC4735815

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Registered trials

None linked

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.