Results 41 to 50 of about 3,141 (147)
Epigenetics & Chromatin, 2023 Background Classical studies on position effect variegation in Drosophila have demonstrated the existence of bi-modal Active/Silent state of the genes juxtaposed to heterochromatin.
Safia Mahabub Sauty, Krassimir Yankulov
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MAPKAP Kinase 2 Blocks Tristetraprolin-directed mRNA Decay by Inhibiting CAF1 Deadenylase Recruitment [PDF]
Journal of Biological Chemistry, 2010 Tristetraprolin (TTP) directs its target AU-rich element (ARE)-containing mRNAs for degradation by promoting removal of the poly(A) tail. The p38 MAPK pathway regulates mRNA stability via the downstream kinase MAPK-activated protein kinase 2 (MAPKAP kinase 2 or MK2), which phosphorylates and prevents the mRNA-destabilizing function of TTP. We show that
Marchese, F +5 more
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Caf1 of Yersinia pestis Forms Complex Highly Stable Protein Polymers and Hydrogel Scaffolds [PDF]
Biophysical Journal, 2016 Caf1 is a polymeric protein from the plague bacterium Y. pestis which is secreted via the chaperone-usher pathway and protects the pathogen from macrophages of the host's immune system by forming a protective layer around the cell. The 15.5kDa monomer has beta structure and resembles the extracellular matrix protein fibronectin.
Waller, Helen +2 more
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EBV Latency Programs: Molecular and Epigenetic Regulation and Its Role in Disease Pathogenesis. [PDF]
J Med VirolABSTRACT Epstein‐Barr virus (EBV) asymptomatically infects over 95% of the global population, and poses a great threat to human health. This review summarizes the complex mechanisms underlying EBV latency programs and their roles in both viral persistence and disease development.
Lyu L, Li Q, Wang C.
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Conservation of the deadenylase activity of proteins of the Caf1 family in human [PDF]
RNA, 2005 The yeast Pop2 protein, belonging to the eukaryotic Caf1 family, is required for mRNA deadenylation in vivo. It also catalyzes poly(A) degradation in vitro, even though this property has been questioned. Caf1 proteins are related to RNase D, a feature supported by the recently published structure of Pop2.
Claire, Bianchin +4 more
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Heterogeneity and complexity within the nuclease module of the Ccr4-Not complex
Frontiers in Genetics, 2013 The shortening of the poly(A) tail of cytoplasmic mRNA (deadenylation) is a pivotal step in the regulation of gene expression in eukaryotic cells. Deadenylation impacts on both regulated mRNA decay as well as the rate of mRNA translation.
Gerlof Sebastiaan Winkler +1 more
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The BTG4 and CAF1 complex prevents the spontaneous activation of eggs by deadenylating maternal mRNAs [PDF]
Open Biology, 2016 Once every menstrual cycle, eggs are ovulated into the oviduct where they await fertilization. The ovulated eggs are arrested in metaphase of the second meiotic division, and only complete meiosis upon fertilization. It is crucial that the maintenance of
Michał Pasternak +3 more
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G3: Genes, Genomes, Genetics, 2018 In “Retrotransposons Are the Major Contributors to the Expansion of the Drosophila ananassae Muller F Element,” Leung et al. (2017) improved contigs attributed to the Muller F element from the original CAF1 assembly, and used them to conclude that most ...
Julie C. Dunning Hotopp, Lisa Klasson
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The Not4 E3 ligase and CCR4 deadenylase play distinct roles in protein quality control. [PDF]
PLoS ONE, 2014 Eukaryotic cells control their proteome by regulating protein production and protein clearance. Protein production is determined to a large extent by mRNA levels, whereas protein degradation depends mostly upon the proteasome.
David Halter +2 more
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Mouse CAF1 Can Function As a Processive Deadenylase/3′–5′-Exonuclease in Vitro but in Yeast the Deadenylase Function of CAF1 Is Not Required for mRNA Poly(A) Removal [PDF]
Journal of Biological Chemistry, 2004 The mouse CAF1 (mCAF1) is an ortholog of the yeast (y) CAF1 protein, which is a component of the CCR4-NOT complex, the major cytoplasmic deadenylase of Saccharomyces cerevisiae. Although CAF1 protein belongs to the DEDDh family of RNases, CCR4 appears to be the principle deadenylase of the CCR4-NOT complex.
Palaniswamy, Viswanathan +4 more
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