Biology subjects

Mallen-Ponce, M. J.

Publications and source records attributed to Mallen-Ponce, M. J..

3 recordsLinked to original sources

bioRxiv2026

Structural determinants underlie the essentiality of the m-type thioredoxin TrxA in Synechocystis

Thioredoxins are central regulators of thiol-based redox signaling in photosynthetic organisms, where multiple isoforms with partially overlapping functions coexist. Among them, TrxA is the cyanobacterial homolog of chloroplast m-type thioredoxins and the only thioredoxin known to be essential in cyanobacteria. However, it is unclear whether this essentiality is due to its high intracellular abundance or to its specific molecular properties. Here, we evaluated the ability of different thioredoxins to functionally replace TrxA and used TrxA/TrxB chimeras to identify the structural determinants underlying its functional specificity. Overexpression of TrxB, TrxQ or TrxC did not support complete segregation of a disrupted trxA locus, although the proteins accumulated to levels comparable to those of endogenous TrxA. Similarly, heterologous expression of NTRC did not rescue the phenotype associated with reduced TrxA levels. Comparative structural analysis revealed differences in surface electrostatics and structural features surrounding the catalytic site of TrxA compared with the other thioredoxins. Analysis of TrxB/TrxA chimeras showed that determinants required for functional complementation are primarily located within the C-terminal region of TrxA. Chimeric variants also differed in their ability to activate cyanobacterial FBP/SBPase and pea chloroplast FBPase in vitro, supporting a role for this region in target-specific interactions. Together, these results demonstrate that the essential function of TrxA cannot be explained by protein abundance alone and requires molecular determinants located primarily within its C-terminal region.

plant biology↗

bioRxiv2026

The cyanobacterium Anabaena uses pleomorphism as an acclimation strategy to high light stress

O_LIPhytoplankton species display characteristic morphologies that are generally assumed to confer adaptive advantages, yet the functional significance of cell shape remains poorly understood. Here, we investigated whether pleomorphism contributes to acclimation to changing light environments. C_LIO_LIUsing the cyanobacterium Anabaena sp. PCC 7120 as a model system, we combined molecular genetics, microscopy, physiological measurements and biophysical analyses to determine how morphology is regulated and how it affects photosynthetic performance under different light intensities. C_LIO_LIWe show that Anabaena undergoes a reversible light-dependent morphological transition from rod-shaped cells under low light to large globular cells under high light stress. This transition is controlled by the relative activities of the elongasome and class A penicillin-binding proteins and is accompanied by thylakoid reorganization. The globular morphology reduces light absorption and enables cells to maintain photosynthetic activity under photoinhibitory conditions. C_LIO_LIOur findings establish a mechanistic link between cell-wall remodelling, cellular optics and photosynthetic performance, revealing pleomorphism as a dynamic acclimation strategy to high light stress. More broadly, this work provides experimental support for the packaging effect and highlights morphology as an active determinant of phytoplankton fitness. C_LI

plant biology↗

bioRxiv2023

Redox-mediated activation of ATG3 promotes ATG8 lipidation and autophagy progression in Chlamydomonas

Autophagy is one of the main degradative pathways used by eukaryotic organisms to eliminate useless or damaged intracellular material in order to maintain cellular homeostasis under stress conditions. Mounting evidence indicates a strong interplay between the generation of ROS and the activation of autophagy. Although a tight redox regulation of autophagy has been shown in several organisms including microalgae, the molecular mechanisms underlying this control remain poorly understood. In this study, we have performed an in-depth in vitro and in vivo redox characterization of ATG3, an E2-activating enzyme involved in ATG8 lipidation and autophagosome formation, from two evolutionary distant unicellular model organisms: the green microalga Chlamydomonas reinhardtii and the budding yeast Saccharomyces cerevisiae. Our results indicated that ATG3 activity from both organisms is subjected to redox regulation since these proteins require reducing equivalents to transfer ATG8 to the phospholipid phosphatidylethanolamine. We established the catalytic Cys of ATG3 as redox target in algal and yeast proteins, and showed that the oxidoreductase thioredoxin efficiently reduces ATG3. Moreover, in vivo studies revealed that the redox state of ATG3 from Chlamydomonas reinhardtii undergoes profound changes in the absence of photoprotective carotenoids, a stress condition that activates autophagy in algae.

plant biology↗