Evidence map›Paper›PMID 12481091›Full record

ArticlePlant physiology2002

The sac mutants of Chlamydomonas reinhardtii reveal transcriptional and posttranscriptional control of cysteine biosynthesis.

Cristina G Ravina, Chwenn-In Chang, George P Tsakraklides, Jeffery P McDermott, Jose M Vega, Thomas Leustek, Cecilia Gotor, John P Davies

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

28 citing papers in PubMed, 81 citations in OpenAlex.

  1. Review
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  6. Fe-S Protein Synthesis in Green Algae Mitochondria.Plants (Basel, Switzerland) · 2021
    Review
  7. Hydrogen sulfide (HaBIOTECH · 2021
    Review
  8. 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

8 authors at 5 institutions in 2 countries.

Cristina G RavinaInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Cientificas, Universidad de Sevilla, 41092 Sevilla, Spain.
Chwenn-In Chang
George P Tsakraklides
Jeffery P McDermott
Jose M Vega
Thomas Leustek
Cecilia Gotor
John P Davies
Rutgers, The State University of New Jersey · USIowa State University · USConsejo Superior de Investigaciones Científicas · ESInstituto de Bioquímica Vegetal y Fotosíntesis · ESUniversidad de Sevilla · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Algae and vascular plants are cysteine (Cys) prototrophs. They are able to import, reduce, and assimilate sulfate into Cys, methionine, and other organic sulfur-containing compounds. Characterization of genes encoding the enzymes required for Cys biosynthesis from the unicellular green alga Chlamydomonas reinhardtii reveals that transcriptional and posttranscriptional mechanisms regulate the pathway. The derived amino acid sequences of the C. reinhardtii genes encoding 5'-adenylylsulfate (APS) reductase and serine (Ser) acetyltransferase are orthologous to sequences from vascular plants. The Cys biosynthetic pathway of C. reinhardtii is regulated by sulfate availability. The steady-state level of transcripts and activity of ATP sulfurylase, APS reductase, Ser acetyltransferase, and O-acetyl-Ser (thiol) lyase increase when cells are deprived of sulfate. The sac1 mutation, which impairs C. reinhardtii ability to acclimate to sulfur-deficient conditions, prevents the increase in accumulation of the transcripts encoding these enzymes and also prevents the increase in activity of all the enzymes except APS reductase. The sac2 mutation, which does not affect accumulation of APS reductase transcripts, blocks the increase in APS reductase activity. These results suggest that APS reductase activity is regulated posttranscriptionally in a SAC2-dependent process.

Indexed as

Multienzyme ComplexesOxidoreductases Acting on Sulfur Group DonorsSaccharomyces cerevisiae ProteinsAcetyltransferasesAnimalsArylsulfatasesCarbon-Oxygen LyasesChlamydomonas reinhardtiiCysteineCysteine SynthaseGene Expression Regulation, EnzymologicMutationOxidoreductasesRNA Processing, Post-TranscriptionalSerine O-AcetyltransferaseSulfate AdenylyltransferaseAcetyltransferasesadenylylsulfate reductaseArylsulfatasesCarbon-Oxygen LyasesCysteineCysteine SynthaseMET17 protein, S cerevisiaeMultienzyme ComplexesO-acetylhomoserine (thiol)-lyaseOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsSaccharomyces cerevisiae ProteinsSerine O-AcetyltransferaseSulfate AdenylyltransferaseSulfatesSulfur

Identifiers

PMID12481091
PMCPMC166719
OpenAlexW1991391971

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.