Member database | Pfam |
Pfam type | family |
Short name | CAF1 |
Clan | RNase_H |
Author | Bateman A;0000-0002-6982-4660 |
Sequence Ontology | 0100021 |
Description
The major pathways of mRNA turnover in eukaryotes initiate with shortening of the polyA tail. CAF1 Swiss:P39008 encodes a critical component of the major cytoplasmic deadenylase in yeast. Both Caf1p is required for normal mRNA deadenylation in vivo and localises to the cytoplasm. Caf1p copurifies with a Ccr4p-dependent polyA-specific exonuclease activity. Some members of this family include and inserted RNA binding domain Pfam:PF01424. This family of proteins is related to other exonucleases Pfam:PF00929 (Bateman A pers. obs.). The crystal structure of Saccharomyces cerevisiae Pop2 (Swiss:P39008) has been resolved at 2.3 Angstrom resolution
[1].
References
1.X-ray structure and activity of the yeast Pop2 protein: a nuclease subunit of the mRNA deadenylase complex. Thore S, Mauxion F, Seraphin B, Suck D. EMBO Rep. 4, 1150-5, (2003). View articlePMID: 14618157
Further reading
2. The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Tucker M, Valencia-Sanchez MA, Staples RR, Chen J, Denis CL, Parker R. Cell 104, 377-86, (2001). View articlePMID: 11239395
3. The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. Korner CG, Wormington M, Muckenthaler M, Schneider S, Dehlin E, Wahle E. EMBO J. 17, 5427-37, (1998). View articlePMID: 9736620
Integrated to
Representative structure
2p51: Crystal structure of the S. pombe Pop2p deadenylation subunit