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- Fedriani, Rubén, 1991, et al.
(författare)
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The SOFIA Massive (SOMA) Star Formation Survey. IV. Isolated Protostars
- 2023
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Ingår i: Astrophysical Journal. - : American Astronomical Society. - 1538-4357 .- 0004-637X. ; 942:1
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Tidskriftsartikel (refereegranskat)abstract
- We present similar to 10-40 mu m SOFIA-FORCAST images of 11 isolated protostars as part of the SOFIA Massive (SOMA) Star Formation Survey, with this morphological classification based on 37 mu m imaging. We develop an automated method to define source aperture size using the gradient of its background-subtracted enclosed flux and apply this to build spectral energy distributions (SEDs). We fit the SEDs with radiative transfer models, developed within the framework of turbulent core accretion (TCA) theory, to estimate key protostellar properties. Here, we release the sedcreator python package that carries out these methods. The SEDs are generally well fitted by the TCA models, from which we infer initial core masses M ( c ) ranging from 20-430 M (circle dot), clump mass surface densities sigma(cl) similar to 0.3-1.7 g cm(-2), and current protostellar masses m (*) similar to 3-50 M (circle dot). From a uniform analysis of the 40 sources in the full SOMA survey to date, we find that massive protostars form across a wide range of clump mass surface density environments, placing constraints on theories that predict a minimum threshold sigma(cl) for massive star formation. However, the upper end of the m (*)-sigma(cl) distribution follows trends predicted by models of internal protostellar feedback that find greater star formation efficiency in higher sigma(cl) conditions. We also investigate protostellar far-IR variability by comparison with IRAS data, finding no significant variation over an similar to 40 yr baseline.
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| 2. |
- Ruiz-Solani, N., et al.
(författare)
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Arabidopsis metacaspase MC1 localizes in stress granules, clears protein aggregates, and delays senescence
- 2023
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Ingår i: Plant Cell. - 1040-4651. ; 35:9, s. 3325-3344
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Tidskriftsartikel (refereegranskat)abstract
- The Arabidopsis metacaspase MC1 is recruited to stress granules upon proteotoxic stress, participates in clearance of pathological protein aggregates, and delays senescence. Stress granules (SGs) are highly conserved cytoplasmic condensates that assemble in response to stress and contribute to maintaining protein homeostasis. These membraneless organelles are dynamic, disassembling once the stress is no longer present. Persistence of SGs due to mutations or chronic stress has been often related to age-dependent protein-misfolding diseases in animals. Here, we find that the metacaspase MC1 is dynamically recruited into SGs upon proteotoxic stress in Arabidopsis (Arabidopsis thaliana). Two predicted disordered regions, the prodomain and the 360 loop, mediate MC1 recruitment to and release from SGs. Importantly, we show that MC1 has the capacity to clear toxic protein aggregates in vivo and in vitro, acting as a disaggregase. Finally, we demonstrate that overexpressing MC1 delays senescence and this phenotype is dependent on the presence of the 360 loop and an intact catalytic domain. Together, our data indicate that MC1 regulates senescence through its recruitment into SGs and this function could potentially be linked to its remarkable protein aggregate-clearing activity.
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