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Agata Malinowska

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Open access Jul 2026

Asparagine-Guided Regulation of Redox Status and Autophagy in Sugar-Starved Lupin (Lupinus spp.) Embryonic Axes—A Transcriptomic and Proteomic Approach

Sugar starvation during seed germination requires coordinated regulation of reserve mobilization, redox homeostasis, and intracellular recycling. In lupin seeds, asparagine is a major nitrogen-rich metabolite, but its role in starvation-induced autophagy and redox regulation remains unclear. Here, isolated embryonic axes of white lupin (Lupinus albus L.) and Andean lupin (Lupinus mutabilis Sweet) were cultured in vitro under sucrose-fed or sugar-starved conditions, with or without asparagine supplementation. Using transcriptomic, proteomic, immunoblot, enzymatic, antioxidant activity, and confocal microscopy analyses, we show that sugar starvation induced redox- and autophagy-related reprogramming, including changes in reactive oxygen species (ROS)-related proteins, catalase accumulation, autophagy-related (ATG) gene expression, vacuolar hydrolase-related responses, and proteolytic activity. Peroxisome-associated components, including glycolate oxidase, acyl-CoA oxidase, and catalase, were strongly affected, indicating dynamic remodeling of peroxisome-related metabolism during starvation. Asparagine modified this response by increasing antioxidant capacity and catalase accumulation under sugar starvation, while reducing detectable autophagosome number, many ATG and vacuolar hydrolase transcripts, and proteolytic activity. Together with previous evidence for asparagine-induced accumulation of autophagic bodies in vacuoles, these results are consistent with asparagine-dependent modulation of several autophagy-related processes rather than with an effect restricted to a single autophagic step. White and Andean lupin shared the same general regulatory framework but differed in response intensity. Thus, asparagine links nitrogen status with redox stabilization, vacuolar catabolism, and autophagy-related dynamics in sugar-starved lupin embryonic axes.

Szymon Stefaniak, Karolina Wleklik, K. Nuc et al. · 0 citations
Open access Aug 2026

Are components of the histone gene expression machinery functionally repurposed in terminally differentiated cells?

The expression of metazoan replication-dependent histone genes is controlled by NPAT and U7 snRNP. NPAT activates transcription of histone genes during S-phase, whereas U7 snRNP is a multi-subunit endonuclease that cleaves the resultant transcripts at the 3' end, yielding mature histone mRNAs. In cycling cells, NPAT and U7 snRNP with its four unique components, U7 snRNA, Lsm10, Lsm11 and FLASH, are highly enriched in Histone Locus Bodies (HLBs), nuclear condensates formed near histone gene loci. Here, we show that in muscle and neural cells that have ceased to replicate their chromatin and permanently exited the cell cycle, HLBs are dismantled and NPAT, FLASH and Lsm11 are detected in the cytoplasm. This observation suggests that in postmitotic cells, NPAT and U7 snRNP become repurposed for functions unrelated to generating histone mRNAs. We identified a highly conserved region in Lsm11 that engages in various protein-protein interactions and likely acts as a universal platform that controls the assembly, localization and function of Lsm11 complexes, including U7 snRNP, during cell growth and differentiation. Since the assembly of U7 snRNP requires SMN, the protein mutated in spinal muscular atrophy (SMA), our results may provide a new perspective on pathophysiology of this neuromuscular disorder.

Xiao-cui Yang, Anthony Desotell, Agata Malinowska et al. · 0 citations
Open access Aug 2026

TTC33 forms a complex with WDR61 and PHF5A to recruit factors relevant to genomic integrity

Using a combination of biochemical assays, structural modeling and molecular dynamics, it is shown that TTC33 directly recruits WDR61 and PHF5A to assemble into a trimeric core complex (TANC), which then forms distinct interactions with either UNG1/2 or SF3B–CCDC97.

R. Tomecki, Małgorzata Drabko, Małgorzata Siek et al. · 0 citations

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