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

RNA. 2010 Jun;16(6):1124-9. doi: 10.1261/rna.2053710. Epub 2010 Apr 19.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatin / genetics
  • Chromatin / metabolism
  • Cycloheximide / metabolism
  • Gene Expression Regulation, Fungal
  • Kinetics
  • Molecular Weight
  • Polynucleotide Adenylyltransferase / chemistry*
  • Polynucleotide Adenylyltransferase / metabolism
  • Polyribosomes / metabolism
  • Puromycin / metabolism
  • RNA, Fungal / genetics
  • RNA, Fungal / metabolism
  • RNA, Ribosomal / genetics
  • RNA, Ribosomal / metabolism
  • Schizosaccharomyces / enzymology
  • Schizosaccharomyces pombe Proteins / chemistry*
  • Schizosaccharomyces pombe Proteins / metabolism

Substances

  • Chromatin
  • RNA, Fungal
  • RNA, Ribosomal
  • Schizosaccharomyces pombe Proteins
  • Puromycin
  • Cycloheximide
  • Cid14 protein, S pombe
  • Polynucleotide Adenylyltransferase