Results 31 to 40 of about 4,758 (202)

The enzyme activities of Caf1 and Ccr4 are both required for deadenylation by the human Ccr4-Not nuclease module [PDF]

open access: yesBiochemical Journal, 2015
In eukaryotic cells, the shortening and removal of the poly(A) tail (deadenylation) of cytoplasmic mRNA is a key event in regulated mRNA degradation. A major enzyme involved in deadenylation is the Ccr4-Not deadenylase complex, which can be recruited to ...
Airhihen, Blessing   +2 more
core   +4 more sources

CCR4 and CAF1 deadenylases have an intrinsic activity to remove the post-poly(A) sequence [PDF]

open access: yesRNA, 2016
MicroRNAs (miRNAs) recruit the CCR4–NOT complex, which contains two deadenylases, CCR4 and CAF1, to promote shortening of the poly(A) tail. Although both CCR4 and CAF1 generally have a strong preference for poly(A) RNA substrates, it has been reported ...
Sho Niinuma, Takashi Fukaya, Y. Tomari
semanticscholar   +3 more sources

The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5 [PDF]

open access: yesMolecular and Cellular Biology, 1999
The CCR4-NOT complex (1 mDa in size), consisting of the proteins CCR4, CAF1, and NOT1 to NOT5, regulates gene expression both positively and negatively and is distinct from other large transcriptional complexes in Saccharomyces cerevisiae such as SNF/SWI,
Chiang, Yueh-Chin   +5 more
core   +4 more sources

1-Hydroxy-xanthine Inhibitors of Caf1 Deadenylase as a Potential Treatment for Osteoporosis [PDF]

open access: yes, 2019
Caf1 is a subunit of the CCR4-NOT complex. The role of Caf1 is that of a magnesium dependent deadenylase enzyme, which removes the poly(A) tail of mRNA (deadenylation).
Ziemann, Max
core   +2 more sources

Histone H3K56 acetylation, CAF1, and Rtt106 coordinate nucleosome assembly and stability of advancing replication forks. [PDF]

open access: yesPLoS Genetics, 2011
Chromatin assembly mutants accumulate recombinogenic DNA damage and are sensitive to genotoxic agents. Here we have analyzed why impairment of the H3K56 acetylation-dependent CAF1 and Rtt106 chromatin assembly pathways, which have redundant roles in H3 ...
Marta Clemente-Ruiz   +2 more
doaj   +1 more source

Caf1 regulates Ash1 histone methyltransferase activity via sensing unmodified histone H3

open access: yesbioRxiv, 2023
Histone modifications are one of key mechanisms to regulate gene expression. Ash1 is a histone H3K36 methyltransferase and involved in gene activation. Ash1 forms a large complex with Mrg15 and Caf1/p55/Nurf55/RbAp48 (AMC complex). Ash1 subunit alone has
Eojin Yoon, Ji-Joon Song
semanticscholar   +1 more source

CCR4-Associated Factor CAF1 Is an Essential Factor for Spermatogenesis [PDF]

open access: yesMolecular and Cellular Biology, 2004
The CCR4-associated protein CAF1 has been demonstrated to play several roles in the control of transcription and of mRNA decay. To gain further insight into its physiological function, we generated CAF1-deficient mice. They are viable, healthy, and normal in appearance; however, mCAF1(-/-) male mice are sterile.
Rouault, Jean-Pierre   +8 more
openaire   +4 more sources

Clonación del gen Caf1 de Yersinia pestis en el Centro Nacional de Productos Biológicos del Instituto Nacional de Salud

open access: yesBoletín Institucional Instituto Nacional de Salud, 2023
Objetivo. Amplificar mediante PCR y clonar la secuencia del gen caf1, que codifica el antígeno capsular F1 de Yersinia pestis, en el plásmido pET 32a (+) de E. coli Top 10 y BL21DE3. Materiales y métodos.
Silvia Seraylán Ormachea   +2 more
semanticscholar   +1 more source

Conservation of the deadenylase activity of proteins of the Caf1 family in human [PDF]

open access: yesRNA, 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
openaire   +2 more sources

Direct Quantification of Protein Antigens in Subunit Plague and Rickettsial Vaccine Preparations

open access: yesПроблемы особо опасных инфекций, 2023
The aim of the work was to put forward the methods for direct quantitative determination of the content of Yersinia pestis and Rickettsia raoultii protein antigens in preparations and various prototypes of subunit vaccines. Materials and methods.
P. Kh. Kopylov, S. V. Dentovskaya
doaj   +1 more source

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