Evidence map›Paper›PMID 21434866›Full record

ArticleThe Biochemical journal2011

Substrate binding disrupts dimerization and induces nucleotide exchange of the chloroplast GTPase Toc33.

Mislav Oreb, Anja Höfle, Patrick Koenig, Maik S Sommer, Irmgard Sinning, Fei Wang, Ivo Tews, Danny J Schnell, Enrico Schleiff

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Chloroplast Omp85 proteins change orientation during evolution.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Mislav OrebCenter for Membrane Proteomics and the Cluster of Excellence Frankfurt, Department of Biosciences, Molecular Cell Biology of Plants, Goethe University Frankfurt, Max-von-Laue Str. 8, D-60438 Frankfurt am Main, Germany.
Anja Höfle
Patrick Koenig
Maik S Sommer
Irmgard Sinning
Fei Wang
Ivo Tews
Danny J Schnell
Enrico Schleiff
Goethe University Frankfurt · DEHeidelberg University · DE

Funding

TOC COMPLEX IN PROTEIN TARGETING TO CHLOROPLASTSR01GM061893 · NIGMS · UNIVERSITY OF MASSACHUSETTS AMHERST · PI SCHNELL, DANNY J. · 2000 to 2014
$3.2M
NIGMS NIH HHS R01 GM061893
6 · The paper itself

Abstract

GTPases act as molecular switches to control many cellular processes, including signalling, protein translation and targeting. Switch activity can be regulated by external effector proteins or intrinsic properties, such as dimerization. The recognition and translocation of pre-proteins into chloroplasts [via the TOC/TIC (translocator at the outer envelope membrane of chloroplasts/inner envelope membrane of chloroplasts)] is controlled by two homologous receptor GTPases, Toc33 and Toc159, whose reversible dimerization is proposed to regulate translocation of incoming proteins in a GTP-dependent manner. Toc33 is a homodimerizing GTPase. Functional analysis suggests that homodimerization is a key step in the translocation process, the molecular functions of which, as well as the elements regulating this event, are largely unknown. In the present study, we show that homodimerization reduces the rate of nucleotide exchange, which is consistent with the observed orientation of the monomers in the crystal structure. Pre-protein binding induces a dissociation of the Toc33 homodimer and results in the exchange of GDP for GTP. Thus homodimerization does not serve to activate the GTPase activity as discussed many times previously, but to control the nucleotide-loading state. We discuss this novel regulatory mode and its impact on the current models of protein import into the chloroplast.

Indexed as

Amino Acid SequenceArabidopsis ProteinsChloroplastsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateMembrane ProteinsMolecular Sequence DataProtein BindingProtein MultimerizationProtein PrecursorsSubstrate SpecificityArabidopsis ProteinsGTP PhosphohydrolasesGuanosine DiphosphateGuanosine TriphosphateMembrane ProteinsProtein PrecursorsToc33 protein, Arabidopsis

Identifiers

PMID21434866
PMCPMC4086448
OpenAlexW2146674824

What OpenQuestion holds

Textmetadata
LicenceTDM
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.