Results 161 to 170 of about 3,723 (183)
Crystal structure and functional properties of the human CCR4-CAF1 deadenylase complex [PDF]
Nucleic Acids Research, 2021 Abstract The CCR4 and CAF1 deadenylases physically interact to form the CCR4-CAF1 complex and function as the catalytic core of the larger CCR4-NOT complex. Together, they are responsible for the eventual removal of the 3′-poly(A) tail from essentially all cellular mRNAs and consequently play a central role in the posttranscriptional ...
Ying Chen +2 more
exaly +13 more sources
Architecture of the Nuclease Module of the Yeast Ccr4-Not Complex: the Not1-Caf1-Ccr4 Interaction [PDF]
Molecular Cell, 2012 Shortening eukaryotic poly(A) tails represses mRNA translation and induces mRNA turnover. The major cytoplasmic deadenylase, the Ccr4-Not complex, is a conserved multisubunit assembly. Ccr4-Not is organized around Not1, a large scaffold protein that recruits two 3'-5' exoribonucleases, Caf1 and Ccr4.
Jérôme Basquin +2 more
exaly +6 more sources
Some of the next articles are maybe not open access.
Related searches:
Related searches:
Tuneable hydrogels of Caf1 protein fibers
Materials Science and Engineering C, 2018Capsular antigen fraction 1 (Caf1) is a robust polymeric protein forming a protective layer around the bacterium Yersinia pestis. Occurring as ≈1 μm polymeric fibers, it shares its immunoglobulin-like fold with the majority of mammalian extracellular proteins such as fibronectin and this structural similarity suggests that this unusual polymer could ...
Gema Dura +2 more
exaly +4 more sources
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.
Yueh-Chin Chiang +2 more
exaly +3 more sources
The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states
Vaccine, 2010Caf1 of the plague bacterium, Yersinia pestis is a polymeric virulence factor and vaccine component, formed from monomers by a donor strand exchange (DSE) mechanism. Here, EM images of Caf1 reveal flexible polymers up to 1.5 microm long (4MDa). The bead-like structures along the polymer are 5.8 + or - 1 nm long and correspond to single Caf1 proteins ...
J Robin Harris, Jeremy H Lakey
exaly +4 more sources
The N-terminus modulates human Caf1 activity, structural stability and aggregation
International Journal of Biological Macromolecules, 2012Caf1 is a deadenylase component of the CCR4-Not complex. Here we found that the removal of the N-terminus resulted in a 30% decrease in human Caf1 (hCaf1) activity, but had no significant influence on main domain structure. The removal of the N-terminus led to a decrease in the thermal stability, while the existence of the N-terminus promoted hCaf1 ...
Likui Feng, Yong-Bin Yan
exaly +3 more sources
Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin [PDF]
Nucleic Acids Research, 2011 The carbon catabolite repressor protein 4 (Ccr4)-Negative on TATA (Not) complex controls gene expression at two levels. In the nucleus, it regulates the basal transcription machinery, nuclear receptor-mediated transcription and histone modifications. In the cytoplasm, the complex is required for messenger RNA (mRNA) turnover through its two associated ...
Georg Stoecklin, Stoecklin Georg
exaly +3 more sources
Novel interaction between CCR4 and CAF1 in rice CCR4–NOT deadenylase complex
Plant Molecular Biology, 2016Rice is an important crop in the world. However, little is known about rice mRNA deadenylation, which is an important regulation step of gene expression at the post-transcriptional level. The CCR4-NOT1 complex contains two key components, CCR4 and CAF1, which are the main cytoplasmic deadenylases in eukaryotic cells.
Wei-Lun, Chou +3 more
openaire +2 more sources
Crystal structures of human BTG2 and mouse TIS21 involved in suppression of CAF1 deadenylase activity [PDF]
Nucleic Acids Research, 2008 BTG2 is the prototypical member of the TOB family and is known to be involved in cell growth, differentiation and DNA repair. As a transcriptional co-regulator, BTG2 interacts with CCR4-associated factor 1 (CAF1) and POP2 (CALIF), which are key components of the general CCR4/NOT multi-subunit transcription complex, and which are reported to play ...
Xiuna Yang +2 more
exaly +3 more sources