Function
Poly(A) RNA polymerase protein Cid1 (Caffeine-Induced Death protein 1) is involved in cell cycle arrest where it inhibits unscheduled mitosis[1]. Cid1 is found in fission yeast. Cid1 exists in 3 forms: apo I consists of 4 subunits; apo II consists of 2 subunits; UTP-bound form consists of 4 subunits.
Poly(A) RNA polymerase Gld2 is responsible for poly(A) tail lengthening. Gld2 activity in the brain is required for long-term memory[2].
Structural highlights
The UTP binding site of Cid1 is between the N-terminal and C-terminal. The active site contains the catalytic triad of aspartic acids (in magenta) in the N-terminal and the His residue (in cyan) whose two conformations select between binding of UTP and ATP to Cid1 [3]. Water molecules are shown as red spheres.
- ↑ Stevenson AL, Norbury CJ. The Cid1 family of non-canonical poly(A) polymerases. Yeast. 2006 Oct 15;23(13):991-1000. PMID:17072891 doi:https://dx.doi.org/10.1002/yea.1408
- ↑ Rouhana L, Wang L, Buter N, Kwak JE, Schiltz CA, Gonzalez T, Kelley AE, Landry CF, Wickens M. Vertebrate GLD2 poly(A) polymerases in the germline and the brain. RNA. 2005 Jul;11(7):1117-30. PMID:15987818 doi:https://dx.doi.org/11/7/1117
- ↑ Yates LA, Fleurdepine S, Rissland OS, De Colibus L, Harlos K, Norbury CJ, Gilbert RJ. Structural basis for the activity of a cytoplasmic RNA terminal uridylyl transferase. Nat Struct Mol Biol. 2012 Jul 1. doi: 10.1038/nsmb.2329. PMID:22751018 doi:10.1038/nsmb.2329