Evidence map›Paper›PMID 18582897›Full record

ArticleJournal of molecular biology2008

Asymmetric nucleotide transactions of the HslUV protease.

Joseph A Yakamavich, Tania A Baker, Robert T Sauer

Abstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing 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

31 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. The HslV Protease fromInternational journal of molecular sciences · 2019
    Article
  6. Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Regulated protein turnover: snapshots of the proteasome in action.Nature reviews. Molecular cell biology · 2014
    Review
  18. Review
  19. Article
  20. Article
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

3 authors.

Joseph A YakamavichDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Tania A Baker
Robert T Sauer

Funding

Systems Biology of Cell Decision ProcessesP50GM068762 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SORGER, PETER KARL · 2003 to 2012
$32.3M
Sequence Determinants of Protein Structure and StabilityR37AI015706 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2002 to 2011
$4.7M
Sequence Determinants of Protein Structure and StabilityR01GM101988 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 2012 to 2019
$3.5M
VIRAL PROTEINS: STRUCTURE AND ASSEMBLY PATHWAYSR01AI015706 · NIAID · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SAUER, ROBERT T · 1985 to 2001
$693k
NIAID NIH HHS AI-15706NIAID NIH HHS R01 AI015706NIAID NIH HHS R37 AI015706NIGMS NIH HHS GM68762NIGMS NIH HHS P50 GM068762NIGMS NIH HHS R01 GM101988
6 · The paper itself

Abstract

ATP binding and hydrolysis are critical for protein degradation by HslUV, a AAA(+) machine containing one or two HslU(6) ATPases and the HslV(12) peptidase. Although each HslU homohexamer has six potential ATP-binding sites, we show that only three or four ATP molecules bind at saturation and present evidence for three functional subunit classes. These results imply that only a subset of HslU and HslUV crystal structures represents functional enzyme conformations. Our results support an asymmetric mechanism of ATP binding and hydrolysis, and suggest that molecular contacts between HslU and HslV vary dynamically throughout the ATPase cycle. Nucleotide binding controls HslUV assembly and activity. Binding of a single ATP allows HslU to bind HslV, whereas additional ATPs must bind HslU to support substrate recognition and to activate ATP hydrolysis, which powers substrate unfolding and translocation. Thus, a simple thermodynamic hierarchy ensures that substrates bind to functional HslUV complexes, that ATP hydrolysis is efficiently coupled to protein degradation, and that working HslUV does not dissociate, allowing highly processive degradation.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid SubstitutionBinding SitesEndopeptidase ClpEscherichia coli ProteinsGlycineHydrolysisKineticsModels, MolecularProtein BindingProtein ConformationProtein Structure, TertiaryProtein SubunitsSubstrate SpecificityAdenosine TriphosphatasesAdenosine TriphosphateClpYQ protease, E coliEndopeptidase ClpEscherichia coli ProteinsGlycineProtein Subunits

Identifiers

PMID18582897
PMCPMC2517146

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.