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Biology subjects

Alonso, M. C.

Publications and source records attributed to Alonso, M. C..

2 recordsLinked to original sources

Seasonal dynamics and thermal vulnerability of marine microbial communities in Uruguayan coastal waters

In an era of accelerating ocean warming, understanding the drivers of microbial community composition is more urgent than ever. Long-term time-series studies are particularly powerful for this purpose. However, most previous work remains confined to the Northern Hemisphere and focuses solely on taxonomy, leaving the Southern Hemisphere underrepresented and microorganisms functional dimensions underexplored. Moreover, phenomena such as current-driven community shifts and microbial vulnerability to warming remain poorly understood. Here, we address these gaps by analyzing microbial communities over two years at the South Atlantic Microbial Observatory (SAMO), located off the coast of Uruguay within a Marine Protected Area. SAMO, situated under the contrasting influences of the Brazil and Malvinas currents and recognized as a global-warming hotspot, provides an ideal setting to study the temporal dynamics of marine microbial communities. Using shotgun metagenomics and 16S rRNA amplicon sequencing, we revealed strong seasonal shifts driven by environmental variability and the influence of these two ocean currents, resulting in two community states (summer-autumn vs winter-spring). These states exhibited contrasting composition, diversity, and assembly mechanisms. Further, our results show that taxonomic and functional diversity trends diverge between these periods. Crucially, our work suggests that the predicted tropicalization of Uruguays coast is likely to boost taxonomic richness but erode functional repertoires, while also increasing vulnerability to ocean warming, potentially undermining biogeochemical functioning.

microbiology↗

Novel class of OTU deubiquitinases regulate substrate ubiquitinationupon Legionella infection

Legionella pneumophila is a gram-negative pathogenic bacterium that causes Legionaries disease. The Legionella genome codes more than 300 effector proteins able to modulate host-pathogen interactions during infection. Among them are also enzymes altering the host-ubiquitination system including bacterial ligases and deubiquitinases. In this study, based on homology-detection screening on 305 Legionella effector proteins, we identified two Legionella OTU-like deubiquitinases (LOT; LotB (Lpg1621/Ceg23) and LotC (Lpg2529), LotA (Lpg2248/Lem21) is already known). A crystal structure of LotC catalytic core (LotC14-310) was determined at 2.4 [A] and compared with other OTU deubiquitinases, including LotB. Unlike the classical OTU-family, the structures of Legionella OTU-family (LotB and LotC) shows an extended helical lobe between the Cys-loop and the variable loop, which define a novel class of OTU-deubiquitinase. Despite structural differences in their helical lobes, both LotB and LotC interact with ubiquitin. LotB has an additional ubiquitin binding site (S1) enabling specific cleavage of Lys63-linked poly-ubiquitin chains. By contrast, LotC only contains the S1 site and cleaves different species of ubiquitin chains. MS analysis of catalytically inactive LotB and LotC identified different categories of host-substrates for these two related DUBs. Together, our results provide new structural insights of bacterial OTU deubiquitinases and indicate distinct roles of bacterial deubiquitinases in host-pathogen interactions.

molecular biology↗