Assembly of the Yeast Exoribonuclease Rrp6 with Its Associated Cofactor Rrp47 Occurs in the Nucleus and Is Critical for the Controlled Expression of Rrp47

Feigenbutz, Monika; Jones, Rosemary; Besong, Tabot M. D.; Harding, Stephen E.; Mitchell, Phil

doi:10.1074/jbc.m112.445759

Cited by 26 publications

(44 citation statements)

References 72 publications

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“…In contrast, Rrp6 expression and nuclear localization are not significantly affected in the rrp47Δ mutant (Stead et al 2007;Feigenbutz et al 2013). Both Rrp47 and the homologous human protein C1D show nucleic acid binding activity in vitro, with a specificity for structured substrates (Schilders et al 2007;Stead et al 2007).…”

Section: Introductionmentioning

confidence: 94%

“…The resultant plasmid (p593) encodes an N-terminal Mpp6 protein fusion bearing two copies of the z domain of protein A from Staphylococcus aureus that is expressed under the control of the RRP4 promoter and also bears the URA3 marker. Analogous constructs expressing a functional N-terminal full-length Rrp6 fusion protein (zz-Rrp6, p263) or rrp6 mutants expressing only the N-terminal 196 aa residues (Rrp6 NT , p287) or expressing the catalytically inactive D238N mutant (Burkard and Butler 2000) (p389) have been described (Allmang et al 1999b;Feigenbutz et al 2013). Constructs encoding the full-length Rrp47 protein (p262) or a C-terminally truncated mutant that encodes the first 120 aa (denoted Rrp47ΔC) (p293) have also been described previously (Costello et al 2011).…”

Section: Plasmidsmentioning

confidence: 99%

“…Csl4-TAP and Rrp6-TAP strains were obtained from Open Biosystems. The rrp47-zz, rrp47-GFP, and rrp47-GFP::HIS3 rrp6Δ::kanMX4 strains have been described (Mitchell et al 2003;Feigenbutz et al 2013). The chromosomally encoded Csl4-TAP, Rrp6-TAP, Rrp47-zz, and Rrp47-GFP fusion protein and the plasmid-encoded Rrp47-TAP fusion proteins were expressed from their homologous promoters.…”

Section: Strainsmentioning

confidence: 99%

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Rrp47 functions in RNA surveillance and stable RNA processing when divorced from the exoribonuclease and exosome-binding domains of Rrp6

Garland

Feigenbutz

Turner

et al. 2013

RNA

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The eukaryotic exosome exoribonuclease Rrp6 forms a complex with Rrp47 that functions in nuclear RNA quality control mechanisms, the degradation of cryptic unstable transcripts (CUTs), and in the 3 ′ end maturation of stable RNAs. Stable expression of Rrp47 is dependent upon its interaction with the N-terminal domain of Rrp6 (Rrp6 NT ). To address the function of Rrp47 independently of Rrp6, we developed a DECOID (decreased expression of complexes by overexpression of interacting domains) strategy to resolve the Rrp6/Rrp47 complex in vivo and employed mpp6Δ and rex1Δ mutants that are synthetic lethal with loss-of-function rrp47 mutants. Strikingly, Rrp47 was able to function in mpp6Δ and rex1Δ mutants when separated from the catalytic and exosome-binding domains of Rrp6, whereas a truncated Rrp47 protein lacking its C-terminal region caused a block in cell growth. Northern analyses of the conditional mutants revealed a specific block in the 3 ′ maturation of box C/D snoRNAs in the rex1 rrp47 mutant and widespread inhibition of Rrp6-mediated RNA surveillance processes in the mpp6 rrp47 mutant. In contrast, growth analyses and RNA northern blot hybridization analyses showed no effect on the rrp47Δ mutant upon overexpression of the Rrp6 NT domain. These findings demonstrate that Rrp47 and Rrp6 have resolvable functions in Rrp6-mediated RNA surveillance and processing pathways. In addition, this study reveals a redundant requirement for Rrp6 or Rex1 in snoRNA maturation and demonstrates the effective use of the DECOID strategy for the resolution and functional analysis of protein complexes.

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Section: Introductionmentioning

confidence: 94%

Section: Plasmidsmentioning

confidence: 99%

Section: Strainsmentioning

confidence: 99%

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Rrp47 functions in RNA surveillance and stable RNA processing when divorced from the exoribonuclease and exosome-binding domains of Rrp6

Garland

Feigenbutz

Turner

et al. 2013

RNA

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“…This was ascribed to a close physical interaction found in vitro between Rrp47p and the N-terminal part of Rrp6p, which may stabilize the Rrp47p protein (22,38,39). Indeed, a Western blot analysis using specific anti-Rrp47p antibodies (Fig.…”

Section: Dis3p Plays Only a Minor Role In The Degradation Of Rhoinducmentioning

confidence: 99%

Cotranscriptional Recruitment of RNA Exosome Cofactors Rrp47p and Mpp6p and Two Distinct Trf-Air-Mtr4 Polyadenylation (TRAMP) Complexes Assists the Exonuclease Rrp6p in the Targeting and Degradation of an Aberrant Messenger Ribonucleoprotein Particle (mRNP) in Yeast

Stuparević¹,

Mosrin-Huaman²,

Hervouet-Coste

et al. 2013

Journal of Biological Chemistry

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Background: Aberrant mRNPs are targeted and degraded by an Rrp6p-dependent nuclear quality control system. Results: The exosome cofactors Rrp47p, Mpp6p, and two TRAMP complexes are cotranscriptionally recruited like Rrp6p and contribute to the elimination process. Conclusion:The exosome cofactors assist Rrp6p in the targeting of aberrant mRNPs. Significance: We provide an integrated view of how cofactors of the RNA degradation machinery cooperate to target aberrant mRNPs.

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“…2b) largely recapitulates the previously determined architecture of the complex. For example, the catalytic subunit Rrp6 is located proximal to Rrp43, Csl4, and Rrp4, predominantly via its CTD(residues 421–676), while its NTD (residues 45–379) is extensively cross-linked to Lrp1 to potentially form a heterodimer 19 (Figs. 2b, 2c).…”

mentioning

confidence: 99%

A strategy for dissecting the architectures of native macromolecular assemblies

et al. 2015

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Despite the central role of large multi-protein complexes in many biological processes, it remains challenging to elucidate their structures and particularly problematic to define the structures of native macromolecular assemblies, which are often of low abundance. Here, we present a strategy for isolating such complexes and for extracting distance restraints that allow the determination of their molecular architectures. The method was optimized to allow facile use of the extensive global resources of GFP-tagged transgenic cells and animals.

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Assembly of the Yeast Exoribonuclease Rrp6 with Its Associated Cofactor Rrp47 Occurs in the Nucleus and Is Critical for the Controlled Expression of Rrp47

Cited by 26 publications

References 72 publications

Rrp47 functions in RNA surveillance and stable RNA processing when divorced from the exoribonuclease and exosome-binding domains of Rrp6

Rrp47 functions in RNA surveillance and stable RNA processing when divorced from the exoribonuclease and exosome-binding domains of Rrp6

Cotranscriptional Recruitment of RNA Exosome Cofactors Rrp47p and Mpp6p and Two Distinct Trf-Air-Mtr4 Polyadenylation (TRAMP) Complexes Assists the Exonuclease Rrp6p in the Targeting and Degradation of an Aberrant Messenger Ribonucleoprotein Particle (mRNP) in Yeast

A strategy for dissecting the architectures of native macromolecular assemblies

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