Publications by authors named "Richard Cardoso da Silva"
The Nucleosome Remodeling and Deacetylation (NuRD) complex is a crucial regulator of cellular differentiation. Two members of the Methyl-CpG-binding domain (MBD) protein family, MBD2 and MBD3, are known to be integral, but mutually exclusive subunits of the NuRD complex. Several MBD2 and MBD3 isoforms are present in mammalian cells, resulting in distinct MBD-NuRD complexes.
View Article and Find Full Text PDFThe generally conserved AAA+ ATPase Pch2/TRIP13 is involved in diverse aspects of meiosis, such as prophase checkpoint function, DNA break regulation, and meiotic recombination. The controlled recruitment of Pch2 to meiotic chromosomes allows it to use its ATPase activity to influence HORMA protein-dependent signaling. Because of the connection between Pch2 chromosomal recruitment and its functional roles in meiosis, it is important to reveal the molecular details that govern Pch2 localization.
View Article and Find Full Text PDFSMAC/DIABLO and HTRA2 are mitochondrial proteins whose amino-terminal sequences, known as inhibitor of apoptosis binding motifs (IBMs), bind and activate ubiquitin ligases known as inhibitor of apoptosis proteins (IAPs), unleashing a cell's apoptotic potential. IBMs comprise a four-residue, loose consensus sequence, and binding to IAPs requires an unmodified amino terminus. Closely related, IBM-like N termini are present in approximately 5% of human proteins.
View Article and Find Full Text PDFBacterial artificial chromosome (BAC)-based transgenes have emerged as a powerful tool for controlled and conditional interrogation of protein function in higher eukaryotes. Although homologous recombination-based recombineering methods have streamlined the efficient integration of protein tags onto BAC transgenes, generating precise point mutations has remained less efficient and time-consuming. Here, we present a simplified method for inserting point mutations into BAC transgenes requiring a single recombineering step followed by antibiotic selection.
View Article and Find Full Text PDFArticle Synopsis
- Pch2 is a specialized protein essential for meiosis, interacting with Orc1, a component of the ORC complex involved in DNA replication.
- This study reveals that Pch2 forms a direct connection with ORC during a specific stage of meiosis, indicating a complex relationship in chromosomal processes that goes beyond mere association with DNA origins.
- The findings suggest that the cooperation between Orc1 and Pch2 in meiosis can occur independently of the usual binding of ORC to DNA replication sites, highlighting unique roles for these proteins in meiotic function.
Article Synopsis
- Pch2 is an AAA+ protein that plays a key role in DNA break formation, recombination, and checkpoint signaling during the meiotic G2/prophase stage in budding yeast.
- The study provides a detailed mapping of where Pch2 associates with the genome, noting that it binds to actively transcribed RNAPII-dependent genes and requires specific factors like Orc1 and the synaptonemal complex component Zip1 for its recruitment.
- The research highlights that while active transcription and Orc1 are important, the recruitment of Pch2 is specifically regulated during meiosis and does not occur in mitotic cells, indicating a unique meiotic licensing mechanism.