cid1 Antibody

1. Data show that a hinge region (N164-N165) of terminal uridylyltransferase Cid1 is essential for catalytic activity. PMID: 25712096
2. Structural analysis of Cid1 bound to a non-hydrolyzable nucleotide UMPNPP and bound to its minimal pseudo-product ApU revealed new key residues for the substrate/product recognition. PMID: 24322298
3. This work demonstrates that Cid1 is able to accommodate all 4 tested ribonucleotide triphosphates (NTP) in the active site, but there are differences in recognition that suggest UTP is the preferred NTP. PMID: 22885303
4. describe crystal structures of cytoplasmic terminal uridylyl transferase Cid1 in apo conformers and bound to UTP, and demonstrate that a single histidine residue, conserved in mammalian Cid1 orthologs, is responsible for discrimination between UTP and ATP PMID: 22751018
5. Cid1 RNA binding properties, a feature with critical implications for miRNAs, histone mRNAs, and, more generally, cellular RNA degradation PMID: 22608966
6. Results describe the biochemical activity of fission yeast Schizosaccharomyces pombe Cid1, a putative cytoplasmic poly(A) polymerase implicated in cell cycle checkpoint controls. PMID: 17353264
7. The Schizosaccharomyces pombe cytoplasmic protein Cid1 acts as a poly(U) polymerase (PUP). Polyadenylated actin mRNA, a target of this activity, is uridylated upon arrest in S phase and is likely to be one of many such Cid1 targets PMID: 18371314

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KEGG: spo:SPAC19D5.03

STRING: 4896.SPAC19D5.03.1