Title: | Red5 and three nuclear pore components are essential for efficient suppression of specific mRNAs during vegetative growth of fission yeast |
Author(s): | Sugiyama T; Wanatabe N; Kitahata E; Tani T; Sugioka-Sugiyama R; |
Address: | "University of Tsukuba, Tsukuba, Ibaraki, 305-8577, Japan. sugiyamt@tara.tsukuba.ac.jp" |
ISSN/ISBN: | 1362-4962 (Electronic) 0305-1048 (Print) 0305-1048 (Linking) |
Abstract: | "Zinc-finger domains are found in many nucleic acid-binding proteins in both prokaryotes and eukaryotes. Proteins carrying zinc-finger domains have important roles in various nuclear transactions, including transcription, mRNA processing and mRNA export; however, for many individual zinc-finger proteins in eukaryotes, the exact function of the protein is not fully understood. Here, we report that Red5 is involved in efficient suppression of specific mRNAs during vegetative growth of Schizosaccharomyces pombe. Red5, which contains five C3H1-type zinc-finger domains, localizes to the nucleus where it forms discrete dots. A red5 point mutation, red5-2, results in the upregulation of specific meiotic mRNAs in vegetative mutant red5-2 cells; northern blot data indicated that these meiotic mRNAs in red5-2 cells have elongated poly(A) tails. RNA-fluorescence in situ hybridization results demonstrate that poly(A)(+) RNA species accumulate in the nucleolar regions of red5-deficient cells. Moreover, Red5 genetically interacts with several mRNA export factors. Unexpectedly, three components of the nuclear pore complex also suppress a specific set of meiotic mRNAs. These results indicate that Red5 function is important to meiotic mRNA degradation; they also suggest possible connections among selective mRNA decay, mRNA export and the nuclear pore complex in vegetative fission yeast" |
Keywords: | "Carrier Proteins/analysis/genetics/*physiology Cell Nucleolus/metabolism Cell Nucleus/chemistry DNA Damage Meiosis/*genetics Mitosis Mutation Nuclear Pore Complex Proteins/*physiology Pheromones Poly(A)-Binding Proteins/genetics Protein Structure, Tertiar;" |
Notes: | "MedlineSugiyama, Tomoyasu Wanatabe, Nobuyoshi Kitahata, Eri Tani, Tokio Sugioka-Sugiyama, Rie eng Research Support, Non-U.S. Gov't England 2013/05/10 Nucleic Acids Res. 2013 Jul; 41(13):6674-86. doi: 10.1093/nar/gkt363. Epub 2013 May 8" |