Proteomic and functional analysis of the noncanonical poly(A) polymerase Cid14
Author(s) -
Claudia Isabelle Keller Valsecchi,
Katrina Woolcock,
Daniel Heß,
Marc Bühler
Publication year - 2010
Publication title -
rna
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.037
H-Index - 171
eISSN - 1469-9001
pISSN - 1355-8382
DOI - 10.1261/rna.2053710
Subject(s) - biology , heterochromatin , computational biology , genetics , chromatin , ribosomal protein , rna polymerase ii , zinc finger , gene , microbiology and biotechnology , ribosome , gene expression , rna , transcription factor , promoter
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.
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