Proteomic and functional analysis of the noncanonical poly(A) polymerase Cid14

• DOI: 10.1261/rna.2053710
• Publication Date: 2010-04-20T03:08:58Z
• Authors: Claudia Keller; Katrina Woolcock; Daniel Hess; Marc Bühler
• Keywords: 0301 basic medicine; Polynucleotide Adenylyltransferase; RNA, Fungal; Chromatin; Molecular Weight; Kinetics; 03 medical and health sciences; RNA, Ribosomal; Gene Expression Regulation, Fungal; Polyribosomes; Schizosaccharomyces; Puromycin; Schizosaccharomyces pombe Proteins; Cycloheximide

The fission yeast Cid14 protein belongs to a family of noncanonical poly(A) polymerases which have been implicated in a broad range of biological functions. Here we describe an extensive Cid14 protein–protein interaction network and its biochemical dissection. Cid14 most stably interacts with the zinc-knuckle protein Air1 to form the Cid14–Air1 complex (CAC). Providing a link to ribosomal RNA processing, Cid14 sediments with 60S ribosomal subunits and copurifies with 60S assembly factors. In contrast, no physical link to chromatin has been identified, although gene expression profiling revealed that efficient silencing of a few heterochromatic genes depends on Cid14 and/or Air1.