Evidence map›Paper›PMID 39612294›Full record

ArticleThe Plant journal : for cell and molecular biology2024

Analysis of the quadruple lsu mutant reveals molecular determinants of the role of LSU proteins in sulfur assimilation in Arabidopsis.

Justyna Piotrowska, Anna Wawrzyńska, Marcin Olszak, Michal Krzyszton, Anastasia Apodiakou, Saleh Alseekh, José María López Ramos, Rainer Hoefgen, Stanislav Kopriva, Agnieszka Sirko

Abstract read
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Article in The Plant journal : for cell and molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

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0cells of the map it votes in
4citing papers in PubMed
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1 · What the graph read from it

What it found

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Justyna PiotrowskaLaboratory of Plant Protein Homeostasis, Institute of Biochemistry and Biophysics Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0001-6135-5110
Anna WawrzyńskaLaboratory of Plant Protein Homeostasis, Institute of Biochemistry and Biophysics Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0002-6985-3904
Marcin OlszakLaboratory of Plant Protein Homeostasis, Institute of Biochemistry and Biophysics Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0003-3375-4506
Michal KrzysztonLaboratory of Seeds Molecular Biology, Institute of Biochemistry and Biophysics Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0002-9795-5588
Anastasia ApodiakouDepartment of Molecular Physiology, Max Planck Institute of Molecular Plant Physiology, Potsdam, Germany.ORCID 0000-0001-9309-5608
Saleh AlseekhDepartment of Molecular Physiology, Max Planck Institute of Molecular Plant Physiology, Potsdam, Germany.ORCID 0000-0003-2067-5235
José María López RamosInstitute for Plant Sciences, Cluster of Excellence on Plant Sciences (CEPLAS), University of Cologne, Cologne, Germany.
Rainer HoefgenDepartment of Molecular Physiology, Max Planck Institute of Molecular Plant Physiology, Potsdam, Germany.ORCID 0000-0001-8590-9800
Stanislav KoprivaInstitute for Plant Sciences, Cluster of Excellence on Plant Sciences (CEPLAS), University of Cologne, Cologne, Germany.ORCID 0000-0002-7416-6551
Agnieszka SirkoLaboratory of Plant Protein Homeostasis, Institute of Biochemistry and Biophysics Polish Academy of Sciences, Warsaw, Poland.ORCID 0000-0002-5205-2924

Funding

Deutsche Forschungsgemeinschaft 426501900Deutsche Forschungsgemeinschaft EXC 2048/1 - project 390686111Deutsche Forschungsgemeinschaft HO1916/13-1Max-Planck-GesellschaftNarodowe Centrum Nauki 2018/31/F/NZ1/02234
6 · The paper itself

Abstract

Because plants are immobile, they have developed intricate mechanisms to sense and absorb nutrients, adjusting their growth and development accordingly. Sulfur is an essential macroelement, but our understanding of its metabolism and homeostasis is limited. LSU (RESPONSE TO LOW SULFUR) proteins are plant-specific proteins with unknown molecular functions and were first identified during transcriptomic studies on sulfur deficiency in Arabidopsis. These proteins are crucial hubs that integrate environmental signals and are involved in the response to various stressors. Herein, we report the direct involvement of LSU proteins in primary sulfur metabolism. Our findings revealed that the quadruple lsu mutant, q-lsu-KO, which was grown under nonlimiting sulfate conditions, exhibited a molecular response resembling that of sulfur-deficient wild-type plants. This led us to explore the interactions of LSU proteins with sulfate reduction pathway enzymes. We found that all LSU proteins interact with ATPS1 and ATPS3 isoforms of ATP sulfurylase, all three isoforms of adenosine 5´ phosphosulfate reductase (APR), and sulfite reductase (SiR). Additionally, in vitro assays revealed that LSU1 enhances the enzymatic activity of SiR. These results highlight the supportive role of LSU proteins in the sulfate reduction pathway.

Indexed as

ArabidopsisArabidopsis ProteinsSulfurGene Expression Regulation, PlantMutationOxidoreductases Acting on Sulfur Group DonorsSulfate AdenylyltransferaseSulfatesArabidopsis ProteinsOxidoreductases Acting on Sulfur Group DonorsSulfate AdenylyltransferaseSulfatesSulfurArabidopsis thalianaLSU (RESPONSE TO LOW SULFUR)sulfate deficiencysulfite reductasesulfur metabolism

Identifiers

PMID39612294
PMCPMC11658185

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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.