Relative contributions of the structural and catalytic roles of Rrp6 in exosomal degradation of individual mRNAs

Mukherjee, K.; Gardin, Justin; Futcher, Bruce; Leatherwood, Janet

doi:10.1261/rna.051490.115

Cited by 11 publications

(14 citation statements)

References 52 publications

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“…The exosome is the main pathway for RNA degradation and is involved in RNA trimming during maturation 40 . The gene rrp6 encodes for a 3′-5′ exo-ribonuclease subunit of the exosome 41 . The deletion of rrp6 resulted in the recovery of TER1 expression in lar7 ∆ cells, close to wild-type level (Fig.…”

Section: Resultsmentioning

confidence: 99%

LARP7 family proteins have conserved function in telomerase assembly

et al. 2018

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Understanding the intricacies of telomerase regulation is crucial due to the potential health benefits of modifying its activity. Telomerase is composed of an RNA component and reverse transcriptase. However, additional factors required during biogenesis vary between species. Here we have identified fission yeast Lar7 as a member of the conserved LARP7 family, which includes the Tetrahymena telomerase-binding protein p65 and human LARP7. We show that Lar7 has conserved RNA-recognition motifs, which bind telomerase RNA to protect it from exosomal degradation. In addition, Lar7 is required to stabilise the association of telomerase RNA with the protective complex LSm2–8, and telomerase reverse transcriptase. Lar7 remains a component of the mature telomerase complex and is required for telomerase localisation to the telomere. Collectively, we demonstrate that Lar7 is a crucial player in fission yeast telomerase biogenesis, similarly to p65 in Tetrahymena, and highlight the LARP7 family as a conserved factor in telomere maintenance.

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Section: Resultsmentioning

confidence: 99%

LARP7 family proteins have conserved function in telomerase assembly

et al. 2018

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“…One line of evidence supporting this is that degradation of poly(A) + transcripts that accumulate in yeast strains lacking Rrp6 can be partially rescued by expressing catalytically inert Rrp6 (Assenholt et al 2008;Mukherjee et al 2016). Furthermore, in vitro studies showed that Rrp6 protein can activate the RNA decay activities of Dis3, especially evident for substrates with poly(A) tails Lima 2012, 2017;Wasmuth et al 2014).…”

Section: Rrp6 Conformations and Rna Pathsmentioning

confidence: 96%

Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors

2017

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The eukaryotic RNA exosome is an essential and conserved protein complex that can degrade or process RNA substrates in the 3 ′ -to-5 ′ direction. Since its discovery nearly two decades ago, studies have focused on determining how the exosome, along with associated cofactors, achieves the demanding task of targeting particular RNAs for degradation and/or processing in both the nucleus and cytoplasm. In this review, we highlight recent advances that have illuminated roles for the RNA exosome and its cofactors in specific biological pathways, alongside studies that attempted to dissect these activities through structural and biochemical characterization of nuclear and cytoplasmic RNA exosome complexes.

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“…Accordingly, when an RNA substrate is engaged in the exosome central channel path to Dis3, Rrp6 is unable to bind another substrate ( 14 ). In addition, Rrp6 appears to contribute to efficient elimination of polyadenylated substrates by Dis3 ( 15 , 16 ).…”

Section: Introductionmentioning

confidence: 99%

Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome

Telekawa

Boisvert

Bachand

2018

Nucleic Acids Research

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The RNA exosome is a conserved multi-subunit complex essential for processing and degradation of several types of RNAs. Although many of the functions of the RNA exosome are well established, whether the activity of this complex is regulated remains unclear. Here we performed a proteomic analysis of the RNA exosome complex purified from Schizosaccharomyces pombe and identified 39 post-translational modifications (PTMs), including phosphorylation, methylation, and acetylation sites. Interestingly, most of the modifications were identified in Dis3, a catalytic subunit of the RNA exosome, as well as in the exosome-associated RNA helicase, Mtr4. Functional analysis of selected PTM sites using modification-deficient and -mimetic versions of exosome subunits revealed substitutions that affected cell growth and exosome functions. Notably, our results suggest that site-specific phosphorylation in the catalytic center of Dis3 and in the helical bundle domain of Mtr4 control their activity. Our findings support a view in which post-translational modifications fine-tune exosome activity and add a layer of regulation to RNA degradation.

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Relative contributions of the structural and catalytic roles of Rrp6 in exosomal degradation of individual mRNAs

Cited by 11 publications

References 52 publications

LARP7 family proteins have conserved function in telomerase assembly

LARP7 family proteins have conserved function in telomerase assembly

Targeting RNA for processing or destruction by the eukaryotic RNA exosome and its cofactors

Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome

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