Evidence map›Paper›PMID 12589070›Full record

ArticleMolecular biology of the cell2003

Pyruvate carboxylase is an essential protein in the assembly of yeast peroxisomal oligomeric alcohol oxidase.

Paulina Ozimek, Ralf van Dijk, Kantcho Latchev, Carlos Gancedo, Dong Yuan Wang, Ida J van der Klei, Marten Veenhuis

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

17 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Moonlighting Proteins: Diverse Functions Found in Fungi.Journal of fungi (Basel, Switzerland) · 2023
    Review
  5. Aerobic Utilization of Methanol for Microbial Growth and Production.Advances in biochemical engineering/biotechnology · 2022
    Article
  6. The N-Acetylglucosamine Kinase fromInternational journal of molecular sciences · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. The Expanding Landscape of Moonlighting Proteins in Yeasts.Microbiology and molecular biology reviews : MMBR · 2016
    Review
  11. Article
  12. Structure and function of biotin-dependent carboxylases.Cellular and molecular life sciences : CMLS · 2013
    Review
  13. Article
  14. Review
  15. Moonlighting proteins in yeasts.Microbiology and molecular biology reviews : MMBR · 2008
    Review
  16. Article
  17. 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

7 authors at 3 institutions in 3 countries.

Paulina OzimekEukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, Haren, The Netherlands.
Ralf van Dijk
Kantcho Latchev
Carlos Gancedo
Dong Yuan Wang
Ida J van der Klei
Marten Veenhuis
University of Groningen · NLBulgarian Academy of Sciences · BGInstituto de Investigaciones Biomédicas Sols-Morreale · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hansenula polymorpha ass3 mutants are characterized by the accumulation of inactive alcohol oxidase (AO) monomers in the cytosol, whereas other peroxisomal matrix proteins are normally activated and sorted to peroxisomes. These mutants also have a glutamate or aspartate requirement on minimal media. Cloning of the corresponding gene resulted in the isolation of the H. polymorpha PYC gene that encodes pyruvate carboxylase (HpPyc1p). HpPyc1p is a cytosolic, anapleurotic enzyme that replenishes the tricarboxylic acid cycle with oxaloacetate. The absence of this enzyme can be compensated by addition of aspartate or glutamate to the growth media. We show that HpPyc1p protein but not the enzyme activity is essential for import and assembly of AO. Similar results were obtained in the related yeast Pichia pastoris. In vitro studies revealed that HpPyc1p has affinity for FAD and is capable to physically interact with AO protein. These data suggest that in methylotrophic yeast pyruvate carboxylase plays a dual role in that, besides its well-characterized metabolic function as anapleurotic enzyme, the protein fulfils a specific role in the AO sorting and assembly process, possibly by mediating FAD-binding to AO monomers.

Indexed as

Aspartic AcidBlotting, WesternCytosolGlutamic AcidHistidineImmunohistochemistryMicroscopy, ElectronMutationPeroxisomesPichiaPlasmidsProtein BindingPyruvate CarboxylaseSpectrometry, FluorescenceTime FactorsAspartic AcidGlutamic AcidHistidinePyruvate Carboxylase

Identifiers

PMID12589070
PMCPMC150008
OpenAlexW2159466931

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.