Evidence map›Paper›PMID 29186573›Full record

ArticleNucleic acids research2018

Conformational dynamics of the Hop1 HORMA domain reveal a common mechanism with the spindle checkpoint protein Mad2.

Alan M V West, Elizabeth A Komives, Kevin D Corbett

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.2field-weighted citation impact, top 7% of its field
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

54 citing papers in PubMed, 93 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The molecular machinery of meiotic recombination.Biochemical Society transactions · 2024
    Review
  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

3 authors at 1 institution in 1 country.

Alan M V WestLudwig Institute for Cancer Research, San Diego Branch, La Jolla, CA 92093, USA.
Elizabeth A KomivesDepartment of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093, USA.
Kevin D CorbettLudwig Institute for Cancer Research, San Diego Branch, La Jolla, CA 92093, USA.
University of California San Diego · US

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAMT32GM008326 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 1989 to 2020
$7.5M
Molecular mechanisms of chromosome organization and recombination control by the meiotic chromosome axis.R01GM104141 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CORBETT, KEVIN DANIEL · 2013 to 2021
$3.1M
NIGMS NIH HHS R01 GM104141NIGMS NIH HHS T32 GM008326
6 · The paper itself

Abstract

The HORMA domain is a highly conserved protein-protein interaction module found in eukaryotic signaling proteins including the spindle assembly checkpoint protein Mad2 and the meiotic HORMAD proteins. HORMA domain proteins interact with short 'closure motifs' in partner proteins by wrapping their C-terminal 'safety belt' region entirely around these motifs, forming topologically-closed complexes. Closure motif binding and release requires large-scale conformational changes in the HORMA domain, but such changes have only been observed in Mad2. Here, we show that Saccharomyces cerevisiae Hop1, a master regulator of meiotic recombination, possesses conformational dynamics similar to Mad2. We identify closure motifs in the Hop1 binding partner Red1 and in Hop1 itself, revealing that HORMA domain-closure motif interactions underlie both Hop1's initial recruitment to the chromosome axis and its self-assembly on the axis. We further show that Hop1 adopts two distinct folded states in solution, one corresponding to the previously-observed 'closed' conformation, and a second more extended state in which the safety belt region has disengaged from the HORMA domain core. These data reveal strong mechanistic similarities between meiotic HORMADs and Mad2, and provide a mechanistic basis for understanding both meiotic chromosome axis assembly and its remodeling by the AAA+ ATPase Pch2/TRIP13.

Indexed as

Protein DomainsAmino Acid SequenceBinding SitesDNA-Binding ProteinsMad2 ProteinsModels, MolecularM Phase Cell Cycle CheckpointsNuclear ProteinsProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidDNA-Binding ProteinsHOP1 protein, S cerevisiaeMad2 ProteinsMAD2 protein, S cerevisiaeNuclear ProteinsPch2 protein, S cerevisiaeRED1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID29186573
PMCPMC5758881
OpenAlexW2768135451

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.