Browsing by Issue Date, starting with "2025-05-08"
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- Editorial: Endocrine disruption in marine species: unraveling pollution and climate change effectsPublication . Bertucci, Juan Ignacio; Blanco, Ayelén Melisa; Estêvão, Maria Dulce da Mota Antunes de OliveiraEndocrine disruption in marine species has emerged as a significant concern in environmental endocrinology, particularly in the context of escalating anthropogenic pressures. Persistent pollutants, including microplastics, heavy metals, and agrochemical residues, alongside climate-induced stressors like ocean warming and acidification, are now recognized as potent modulators of endocrine function in aquatic organisms. These stressors compromise critical physiological and behavioral processes, with potential implications for individual fitness, population viability, and ecosystem stability. The Research Topic Endocrine disruption in marine species: unraveling pollution and climate change effects brings together a multidisciplinary set of contributions that examine the mechanistic underpinnings, organismal impacts, and ecological implications of endocrine disruption across marine taxa. This editorial synthesizes the key findings, contextualizes them within the broader scientific discourse, and highlights knowledge gaps and future research directions.
- The α5-α6-α7-Pba3-Pba4 complex: a starting unit in proteasome core particle assemblyPublication . Matias, Ana Catarina; Tiago, Maria Margarida; Zimmermann, Jessica; Dohmen, R. Jürgen; Ramos, Paula C.A complex composed of Pba3-Pba4 and subunits α5, α6, and α7 is identified as an early intermediate in proteasome core particle assembly in wild-type Saccharomyces cerevisiae cells. The same complex can be reconstituted from recombinantly produced components in vitro. Assembly of α6 and α7 with Pba3-Pba4 depends on the presence of the α5 subunit, the binding of which apparently initiates the formation of this intermediate. Our data suggest the following order of events: first, Pba3-Pba4 binds α5, then α6 is incorporated, and at the end α7. In the absence of the chaperones Pba1-Pba2 or Ump1, alternative Pba4-containing complexes are detected, the formation of which depends on the Blm10/PA200 protein. Overexpression of Pba1-Pba2 abolishes the formation of these complexes containing Pba4 and Blm10, suggesting that Blm10 may replace Pba1-Pba2 as an alternative assembly factor.