Evidence map›Paper›PMID 25336638›Full record

ArticleThe Journal of biological chemistry2014

Characterization and interaction studies of two isoforms of the dual localized 3-mercaptopyruvate sulfurtransferase TUM1 from humans.

Benjamin Fräsdorf, Christin Radon, Silke Leimkühler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 19% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 79 citations in OpenAlex.

  1. Old and Promising Markers Related to Autophagy in Traumatic Brain Injury.International journal of molecular sciences · 2022
    Pooled it
  2. Review
  3. Article
  4. Review
  5. Review
  6. Hydrogen Sulfide (HBiomolecules · 2024
    Review
  7. Hydrogen sulfide and its role in female reproduction.Frontiers in veterinary science · 2024
    Review
  8. Review
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Hydrogen Sulfide Biology and Its Role in Cancer.Molecules (Basel, Switzerland) · 2022
    Review
  15. Article
  16. Sulfur Administration in Fe-S Cluster Homeostasis.Antioxidants (Basel, Switzerland) · 2021
    Review
  17. Review
  18. Review
  19. Review
  20. Urm1: A Non-Canonical UBL.Biomolecules · 2021
    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.

Benjamin FräsdorfFrom the University of Potsdam, Institute of Biochemistry and Biology, D-14476 Potsdam, Germany.
Christin RadonFrom the University of Potsdam, Institute of Biochemistry and Biology, D-14476 Potsdam, Germany.
Silke LeimkühlerFrom the University of Potsdam, Institute of Biochemistry and Biology, D-14476 Potsdam, Germany sleim@uni-potsdam.de.
University of Potsdam · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human tRNA thiouridine modification protein (TUM1), also designated as 3-mercaptopyruvate sulfurtransferase (MPST), has been implicated in a wide range of physiological processes in the cell. The roles range from an involvement in thiolation of cytosolic tRNAs to the generation of H2S as signaling molecule both in mitochondria and the cytosol. TUM1 is a member of the sulfurtransferase family and catalyzes the conversion of 3-mercaptopyruvate to pyruvate and protein-bound persulfide. Here, we purified and characterized two novel TUM1 splice variants, designated as TUM1-Iso1 and TUM1-Iso2. The purified proteins showed similar kinetic behavior and comparable pH and temperature dependence. Cellular localization studies, however, showed a different localization pattern between the isoforms. TUM1-Iso1 is exclusively localized in the cytosol, whereas TUM1-Iso2 showed a dual localization both in the cytosol and mitochondria. Interaction studies were performed with the isoforms both in vitro using the purified proteins and in vivo by fluorescence analysis in human cells, using the split-EGFP system. The studies showed that TUM1 interacts with the l-cysteine desulfurase NFS1 and the rhodanese-like protein MOCS3, suggesting a dual function of TUM1 both in sulfur transfer for the biosynthesis of the molybdenum cofactor, and for the thiolation of tRNA. Our studies point to distinct roles of each TUM1 isoform in the sulfur transfer processes in the cell, with different compartmentalization of the two splice variants of TUM1.

Indexed as

Amino Acid SequenceCarbon-Sulfur LyasesCytosolGreen Fluorescent ProteinsHEK293 CellsHumansHydrogen-Ion ConcentrationIsoenzymesKineticsMitochondriaMolecular Sequence DataNucleotidyltransferasesProtein BindingProtein TransportSulfurSulfurtransferases3-mercaptopyruvate sulphurtransferaseCarbon-Sulfur Lyasesenhanced green fluorescent proteinGreen Fluorescent ProteinsIsoenzymesMOCS3 protein, humanNFS1 protein, humanNucleotidyltransferasesSulfurSulfurtransferasesFluorescenceMitochondriaMolybdenumSulfurTransfer RNA (tRNA)

Identifiers

PMID25336638
PMCPMC4263862
OpenAlexW2017545901

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.