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.
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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Who cites it
4 citing papers in PubMed.
- Hidden players in plant response to sulfur deficit and beyond: insights into the function of the proteins Sulfur Deficiency Induced and Response to Low Sulfur.Journal of experimental botany · 2026Review
- Comparative Transcriptomic Analysis Reveals Conserved and Nutrient-Specific Responses to Nutrient Deficiencies in Quinoa.Plants (Basel, Switzerland) · 2026Article
- Review
- Short coiled-coil proteins from plants and metazoans - the 'jacks of all trades'.The FEBS journal · 2025Review
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Authors and funding
10 authors.
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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.
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