Evidence map›Paper›PMID 22730323›Full record

ArticleThe Journal of biological chemistry2012

Mitochondrial cysteine synthase complex regulates O-acetylserine biosynthesis in plants.

Markus Wirtz, Katherine F M Beard, Chun Pong Lee, Achim Boltz, Markus Schwarzländer, Christopher Fuchs, Andreas J Meyer, Corinna Heeg, Lee J Sweetlove, R George Ratcliffe and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
3.1field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
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  10. Metabolism and Regulatory Functions ofFrontiers in plant science · 2021
    Review
  11. Chloroplast-associated molecular patterns as concept for fine-tuned operational retrograde signalling.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020
    Review
  12. Article
  13. Article
  14. The PhotorespiratoryFrontiers in plant science · 2018
    Article
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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

11 authors at 2 institutions in 2 countries.

Markus WirtzCentre for Organismal Studies (COS) Heidelberg, University of Heidelberg, Im Neuenheimer Feld 360, 69120 Heidelberg, Germany.
Katherine F M Beard
Chun Pong Lee
Achim Boltz
Markus Schwarzländer
Christopher Fuchs
Andreas J Meyer
Corinna Heeg
Lee J Sweetlove
R George Ratcliffe
Rüdiger Hell
Heidelberg University · DEUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

Cysteine synthesis is catalyzed by serine acetyltransferase (SAT) and O-acetylserine (thiol) lyase (OAS-TL) in the cytosol, plastids, and mitochondria of plants. Biochemical analyses of recombinant plant SAT and OAS-TL indicate that the reversible association of the proteins in the cysteine synthase complex (CSC) controls cellular sulfur homeostasis. However, the relevance of CSC formation in each compartment for flux control of cysteine synthesis remains controversial. Here, we demonstrate the interaction between mitochondrial SAT3 and OAS-TL C in planta by FRET and establish the role of the mitochondrial CSC in the regulation of cysteine synthesis. NMR spectroscopy of isolated mitochondria from WT, serat2;2, and oastl-C plants showed the SAT-dependent export of OAS. The presence of cysteine resulted in reduced OAS export in mitochondria of oastl-C mutants but not in WT mitochondria. This is in agreement with the stronger in vitro feedback inhibition of free SAT by cysteine compared with CSC-bound SAT and explains the high OAS export rate of WT mitochondria in the presence of cysteine. The predominant role of mitochondrial OAS synthesis was validated in planta by feeding [(3)H]serine to the WT and loss-of-function mutants for OAS-TLs in the cytosol, plastids, and mitochondria. On the basis of these results, we propose a new model in which the mitochondrial CSC acts as a sensor that regulates the level of SAT activity in response to sulfur supply and cysteine demand.

Indexed as

Models, BiologicalArabidopsisArabidopsis ProteinsBiological TransportCysteineCysteine SynthaseMagnetic Resonance SpectroscopyMitochondriaMitochondrial ProteinsSerineSerine O-AcetyltransferaseArabidopsis ProteinsCysteineCysteine SynthaseMitochondrial ProteinsO-acetylserineSerineSerine O-Acetyltransferase

Identifiers

PMID22730323
PMCPMC3431704
OpenAlexW2073137883

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.