RNAi in fission yeast finds new targets and new ways of targeting at the nuclear periphery: Figure 1.

Holoch, Daniel; Moazed, Danesh

doi:10.1101/gad.191155.112

Cited by 6 publications

(5 citation statements)

References 33 publications

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“…2c). This observation complements the finding that RNAi in S. pombe acts primarily to silence heterochromatin-bound RNAs and read through antisense transcripts [42]. In S. pombe , heterochromatin is formed predominantly at centromeres and telomeres.…”

Section: Eri1 Regulation Of Small Rnassupporting

confidence: 84%

Eri1: a conserved enzyme at the crossroads of multiple RNA-processing pathways

Thomas¹,

L’Étoile²,

Ansel³

2014

Trends in Genetics

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Eri1 is an evolutionarily conserved 3′–5′ exoribonuclease that participates in 5.8S rRNA 3′ end processing and turnover of replication-dependent histone mRNAs. Over the course of evolution, Eri1 has also been recruited into a variety of conserved and species-specific regulatory small RNA pathways that include endogenous small interfering RNAs and microRNAs. Recent advances in Eri1 biology illustrate the importance of RNA metabolism in epigenetic gene regulation and illuminate common principles and players in RNA biogenesis and turnover. In this review, we highlight Eri1 as a member of a growing class of ribosome- and histone mRNA-associated proteins that have been recruited into divergent RNA metabolic pathways. We summarize recent advances in the understanding of Eri1 function in these pathways and discuss how Eri1 impacts gene expression and physiology in a variety of eukaryotic species. This emerging view highlights the possibility for crosstalk and coregulation of diverse cellular processes regulated by RNA.

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Section: Eri1 Regulation Of Small Rnassupporting

confidence: 84%

Eri1: a conserved enzyme at the crossroads of multiple RNA-processing pathways

Thomas¹,

L’Étoile²,

Ansel³

2014

Trends in Genetics

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“…NRDE-2 is directed to nascent transcripts through association with an siRNA-incorporated Argonaut (AGO) protein, NRDE-3, to introduce H3K9 methylation and block RNAP II elongation [7]. Although no RNAi factors were identified in the NRDE-2 (Nrl1)-proteomics analysis performed by us (human) and others (yeast), RNAi factor-directed introduction of H3K9me is observed in both organisms [15,36]. Notably, there are interconnections between R loops and the modification status of chromatin (reviewed by [37,38]).…”

Section: Discussionmentioning

confidence: 99%

NRDE-2, the human homolog of fission yeast Nrl1, prevents DNA damage accumulation in human cells

et al. 2018

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The RNA helicase Mtr4 is a versatile protein that is a crucial component of several distinct RNA surveillance complexes. Here we describe a novel complex that contains Mtr4, but has a role distinct from any of those previously described. We found that Mtr4 association with the human homolog of fission yeast Nrl1, NRDE-2, defines a novel function for Mtr4 in the DNA damage response pathway. We provide biochemical evidence that Mtr4 and NRDE-2 are part of the same complex and show that both proteins play a role in the DNA damage response by maintaining low DNA double-strand break levels. Importantly, the DNA damage response function of the Mtr4/NRDE-2 complex does not depend on the formation of R loops. We show however that NRDE-2 and Mtr4 can affect R-loop signals at a subset of distinct genes, possibly regulating their expression. Our work not only expands the wide range of Mtr4 functions, but also elucidates an important role of the less characterized human NRDE-2 protein.

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“…Temperature-induced loss of nuclear-pore-associated Dcr1 provides an elegant mechanism for the release of BANC genes from RNAi repression under temperature stress (Holoch and Moazed, 2012). However, it raises two important questions: how is aggregation of Dcr1 prevented and, given the loss of nuclear Dcr1, what ensures the integrity of centromeric heterochromatin at elevated temperatures?…”

Section: Introductionmentioning

confidence: 99%

Dicer and Hsp104 Function in a Negative Feedback Loop to Confer Robustness to Environmental Stress

et al. 2015

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Epigenetic mechanisms can be influenced by environmental cues and thus evoke phenotypic variation. This plasticity can be advantageous for adaptation but also detrimental if not tightly controlled. Although having attracted considerable interest, it remains largely unknown if and how environmental cues such as temperature trigger epigenetic alterations. Using fission yeast, we demonstrate that environmentally induced discontinuous phenotypic variation is buffered by a negative feedback loop that involves the RNase Dicer and the protein disaggregase Hsp104. In the absence of Hsp104, Dicer accumulates in cytoplasmic inclusions and heterochromatin becomes unstable at elevated temperatures, an epigenetic state inherited for many cell divisions after the heat stress. Loss of Dicer leads to toxic aggregation of an exogenous prionogenic protein. Our results highlight the importance of feedback regulation in building epigenetic memory and uncover Hsp104 and Dicer as homeostatic controllers that buffer environmentally induced stochastic epigenetic variation and toxic aggregation of prionogenic proteins.

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RNAi in fission yeast finds new targets and new ways of targeting at the nuclear periphery: Figure 1.

Cited by 6 publications

References 33 publications

Eri1: a conserved enzyme at the crossroads of multiple RNA-processing pathways

Eri1: a conserved enzyme at the crossroads of multiple RNA-processing pathways

NRDE-2, the human homolog of fission yeast Nrl1, prevents DNA damage accumulation in human cells

Dicer and Hsp104 Function in a Negative Feedback Loop to Confer Robustness to Environmental Stress

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