Publications by authors named "Caio A Rebula"
Article Synopsis
- Dss1 is a conserved and intrinsically disordered protein with multiple functions, including roles in protein degradation, DNA repair, transcription, and mRNA export.
- It interacts with several complexes, such as BRCA2 and the COP9 signalosome, and in Schizosaccharomyces pombe, its interactome is further expanded to include eIF3 and mitotic septins.
- The protein features a dynamic C-terminal helix that influences binding interactions, notably enhancing septin binding while interfering with ATP-citrate lyase, suggesting that Dss1's transient interactions can significantly alter its functional relationships.
DSS1/Sem1 is a versatile intrinsically disordered protein. Besides being a bona fide subunit of the 26S proteasome, DSS1 associates with other protein complexes, including BRCA2-RPA, involved in homologous recombination; the Csn12-Thp3 complex, involved in RNA splicing; the integrator, involved in transcription; and the TREX-2 complex, involved in nuclear export of mRNA and transcription elongation. As a subunit of the proteasome, DSS1 functions both in complex assembly and possibly as a ubiquitin receptor.
View Article and Find Full Text PDFIn their natural environment, cells are regularly exposed to various stress conditions that may lead to protein misfolding, but also in the absence of stress, misfolded proteins occur as the result of mutations or failures during protein synthesis. Since such partially denatured proteins are prone to aggregate, cells have evolved several elaborate quality control systems to deal with these potentially toxic proteins. First, various molecular chaperones will seize the misfolded protein and either attempt to refold the protein or target it for degradation via the ubiquitin-proteasome system.
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