Evidence map›Paper›PMID 26371297›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structure of subcomplex Iβ of mammalian respiratory complex I leads to new supernumerary subunit assignments.

Jiapeng Zhu, Martin S King, Minmin Yu, Liron Klipcan, Andrew G W Leslie, Judy Hirst

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Plant direct · 2020
    Article
  10. Article
  11. Article
  12. Impaired Mitochondrial Fatty Acid Synthesis Leads to Neurodegeneration in Mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Subunit NDUFV3 is present in two distinct isoforms in mammalian complex I.Biochimica et biophysica acta. Bioenergetics · 2017
    Article
  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

6 authors.

Jiapeng ZhuMedical Research Council Mitochondrial Biology Unit, Cambridge, CB2 0XY, United Kingdom;
Martin S KingMedical Research Council Mitochondrial Biology Unit, Cambridge, CB2 0XY, United Kingdom;
Minmin YuMedical Research Council Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom.
Liron KlipcanMedical Research Council Mitochondrial Biology Unit, Cambridge, CB2 0XY, United Kingdom;
Andrew G W LeslieMedical Research Council Laboratory of Molecular Biology, Cambridge, CB2 0QH, United Kingdom.
Judy HirstMedical Research Council Mitochondrial Biology Unit, Cambridge, CB2 0XY, United Kingdom; jh@mrc-mbu.cam.ac.uk.

Funding

Medical Research Council MC_U105184325Medical Research Council MC_U105663141Medical Research Council U105184325Medical Research Council U105663141
6 · The paper itself

Abstract

Mitochondrial complex I (proton-pumping NADH:ubiquinone oxidoreductase) is an essential respiratory enzyme. Mammalian complex I contains 45 subunits: 14 conserved "core" subunits and 31 "supernumerary" subunits. The structure of Bos taurus complex I, determined to 5-Å resolution by electron cryomicroscopy, described the structure of the mammalian core enzyme and allowed the assignment of 14 supernumerary subunits. Here, we describe the 6.8-Å resolution X-ray crystallography structure of subcomplex Iβ, a large portion of the membrane domain of B. taurus complex I that contains two core subunits and a cohort of supernumerary subunits. By comparing the structures and composition of subcomplex Iβ and complex I, supported by comparisons with Yarrowia lipolytica complex I, we propose assignments for eight further supernumerary subunits in the structure. Our new assignments include two CHCH-domain containing subunits that contain disulfide bridges between CX9C motifs; they are processed by the Mia40 oxidative-folding pathway in the intermembrane space and probably stabilize the membrane domain. We also assign subunit B22, an LYR protein, to the matrix face of the membrane domain. We reveal that subunit B22 anchors an acyl carrier protein (ACP) to the complex, replicating the LYR protein-ACP structural module that was identified previously in the hydrophilic domain. Thus, we significantly extend knowledge of how the mammalian supernumerary subunits are arranged around the core enzyme, and provide insights into their roles in biogenesis and regulation.

Indexed as

CattleModels, MolecularAnimalsCryoelectron MicroscopyElectron Transport Complex IProtein ConformationProtein SubunitsYarrowiaElectron Transport Complex IProtein SubunitsCHCH domainelectron transport chainLYR proteinmitochondriaNADH:ubiquinone oxidoreductase

Identifiers

PMID26371297
PMCPMC4593082

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.