AIP1 is a novel Agenet/Tudor domain protein from Arabidopsis that interacts with regulators of DNA replication, transcription and chromatin remodeling [PDF]
Background: DNA replication and transcription are dynamic processes regulating plant development that are dependent on the chromatin accessibility. Proteins belonging to the Agenet/Tudor domain family are known as histone modification "readers" and ...
Barroso-Neto, Ito Liberato +9 more
core +3 more sources
Multiple ETS family transcription factors bind mutant p53 via distinct interaction regions
Mutant p53 gain‐of‐function is thought to be mediated by interaction with other transcription factors. We identify multiple ETS transcription factors that can bind mutant p53 and found that this interaction can be promoted by a PXXPP motif. ETS proteins that strongly bound mutant p53 were upregulated in ovarian cancer compared to ETS proteins that ...
Stephanie A. Metcalf +6 more
wiley +1 more source
Orthoflaviviruses remodel the endoplasmic reticulum (ER) network to construct replication organelles (ROs) for RNA replication. In this study, we demonstrate that the Japanese encephalitis virus (JEV) NS1 protein concentrates ER membranes in the ...
Shengda Xie +6 more
doaj +1 more source
Assembly-hub function of ER-localized SNARE proteins in biogenesis of tombusvirus replication compartment. [PDF]
Positive-strand RNA viruses assemble numerous membrane-bound viral replicase complexes within large replication compartments to support their replication in infected cells. Yet the detailed mechanism of how given subcellular compartments are subverted by
Zsuzsanna Sasvari +4 more
doaj +1 more source
Mycophenolic acid (MPA) modulates host cellular autophagy progression in sub genomic dengue virus-2 replicon cells [PDF]
Cellular autophagy (Macrophagy) is a self-degradative process, executed through the network of autophagy associated genes (ATGs) encoded proteins. Both in vitro and in vivo studies suggest that dengue virus (DENV) induces autophagy and supports the viral
Dungdung, Ranjeet +4 more
core +1 more source
Replication protein A is sequentially phosphorylated during meiosis [PDF]
Phosphorylation of the cellular single-stranded DNA-binding protein, replication protein A (RPA), occurs during normal mitotic cell cycle progression and also in response to genotoxic stress. In budding yeast, these reactions require the ATM homolog Mec1, a central regulator of the DNA replication and DNA damage checkpoint responses. We now demonstrate
G S, Brush +3 more
openaire +2 more sources
The newfound relationship between extrachromosomal DNAs and excised signal circles
Extrachromosomal DNAs (ecDNAs) contribute to the progression of many human cancers. In addition, circular DNA by‐products of V(D)J recombination, excised signal circles (ESCs), have roles in cancer progression but have largely been overlooked. In this Review, we explore the roles of ecDNAs and ESCs in cancer development, and highlight why these ...
Dylan Casey, Zeqian Gao, Joan Boyes
wiley +1 more source
Identifying Interaction Sites in "Recalcitrant" Proteins: Predicted Protein and Rna Binding Sites in Rev Proteins of Hiv-1 and Eiav Agree with Experimental Data [PDF]
Protein-protein and protein nucleic acid interactions are vitally important for a wide range of biological processes, including regulation of gene expression, protein synthesis, and replication and assembly of many viruses.
Carpenter, Susan +8 more
core +3 more sources
Detection of Posttranslational Modifications of Replication Protein A [PDF]
Replication Protein A (RPA) is a single-strand DNA-binding protein that is found in all eukaryotes. RPA is subjected to multiple posttranslational modifications including serine- and threonine-phosphorylation, poly-ADP ribosylation, and SUMOylation. These modifications are believed to regulate RPA activity through modulating interactions with DNA and ...
Cathy S, Hass, Ran, Chen, Marc S, Wold
openaire +2 more sources
This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva +5 more
wiley +1 more source

