Abstract

Accurate target recognition in transcript degradation is crucial for regulation of gene expression. In the fission yeast Schizosaccharomyces pombe, a number of meiotic transcripts are recognized by a YTH-family RNA-binding protein, Mmi1, and selectively degraded by the nuclear exosome during mitotic growth. Mmi1 forms nuclear foci in mitotically growing cells, and the nuclear exosome colocalizes to such foci. However, it remains elusive how Mmi1 and the nuclear exosome are connected. Here, we show that a complex called MTREC (Mtl1-Red1 core) or NURS (nuclear RNA silencing) that consists of a zinc-finger protein, Red1, and an RNA helicase, Mtl1, is required for the recruitment of the nuclear exosome to Mmi1 foci. Physical interaction between Mmi1 and the nuclear exosome depends on Red1. Furthermore, a chimeric protein involving Mmi1 and Rrp6, which is a nuclear-specific component of the exosome, suppresses the ectopic expression phenotype of meiotic transcripts in red1Δ cells and mtl1 mutant cells. These data indicate that the primary function of MTREC/NURS in meiotic transcript elimination is to link Mmi1 to the nuclear exosome physically.

Highlights

  • Stability control of transcripts is crucial to establish appropriate gene expression profiles in a wide range of biological processes [1, 2]

  • In the fission yeast Schizosaccharomyces pombe, selective degradation of meiotic transcripts is employed to prevent their deleterious expression during mitotic

  • MTREC recruits the nuclear exosome to YTH-RNA-binding protein mutant cells lacking the self-interaction domain (SID) and erh1 deletion mutant cells do not form Mmi1 foci

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Summary

Introduction

Stability control of transcripts is crucial to establish appropriate gene expression profiles in a wide range of biological processes [1, 2]. Mmi1-mediated selective elimination of meiotic transcripts requires polyadenylation-related factors, including a canonical poly(A) polymerase, Pla, and a poly(A)-binding protein, Pab2 [12, 19, 20]. Another pivotal factor engaged in Mmi1-mediated RNA degradation is a zinc-finger protein, Red1 [21, 22]. The machinery of Mmi1-mediated RNA degradation triggers facultative heterochromatin formation at a subset of its target genes [5, 26, 27] It regulates transcription termination of its targets [28,29,30], suggesting that Mmi1-mediated multilayered regulation rigorously shapes appropriate gene expression profiles in mitotically growing cells

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