Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus

Witharana, Chamindri; Roppelt, Verena; Lochnit, Günther; Klug, Gabriele; Evguenieva‐Hackenberg, Elena

doi:10.1016/j.biochi.2012.03.026

Cited by 24 publications

(61 citation statements)

References 47 publications

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“…Sul7d and Cren7 were purified as described (25,37). Rrp4-exosome and Csl4-exosome complexes were reconstituted using purified subunits as described (39). Mutant proteins were expressed and purified by a procedure identical to the one for their wild-type proteins.…”

Section: Methodsmentioning

confidence: 99%

“…B, heterogeneous complexes of RNA exosome proteins are differently methylated by aKMT4. Two exosome complexes, Rrp4-exosome (Rrp42/41/ Rrp4) and Csl4-exosome (Rrp42/41/Csl4), were reconstituted in vitro using purified recombinant proteins, as described by Witharana et al (39). Note that the methylation of Rrp42 in Rrp4-exosome and Csl4 in Csl4-exosome was greatly reduced.…”

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

“…One of the best studied complexes in Sulfolobus is the RNA exosome, which is responsible for RNA processing and degradation (39,46). The archaeal exosome consists of only four proteins with structurally similarity to the eukaryotic exosome core.…”

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

“…The catalytically active Rrp41 and its structural partner Rrp42 form a hexameric ring. Rrp4 (or Csl4) forms a trimeric cap on one side of the ring for RNA substrate binding (39). Taking advantage of the existence of heterogeneous complexes of the exosome in Sulfolobus, we examined how aKMT4 works on protein complex substrates.…”

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

“…Taking advantage of the existence of heterogeneous complexes of the exosome in Sulfolobus, we examined how aKMT4 works on protein complex substrates. The two forms of exosome complex, called Rrp4-exosome and Csl4-exosome, were reconstituted in vitro using purified recombinant proteins (39). Intriguingly, when they were subjected to MTase assays alongside each individual subunit, different methylation patterns could be seen (Fig.…”

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

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A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

Niu

Xia

Wang

et al. 2013

Journal of Biological Chemistry

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Background:The origin of eukaryotic histone modification enzymes still remains obscure. Results: Prototypic KMT4/Dot1 from Archaea targets chromatin proteins (Sul7d and Cren7) and shows increased activity on Sul7d, but not Cren7, in the presence of DNA. Conclusion: Promiscuous aKMT4 could be regulated by chromatin environment. Significance: This study supports the prokaryotic origin model of eukaryotic histone methyltransferases and sheds light on chromatin dynamics in Archaea.

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Section: Methodsmentioning

confidence: 99%

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

Section: Dot1-like Proteins Are Widespread In Crenarchaea and Somementioning

confidence: 99%

See 3 more Smart Citations

A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

Niu

Xia

Wang

et al. 2013

Journal of Biological Chemistry

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Nop5 interacts with the archaeal RNA exosome

et al. 2017

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The archaeal exosome, a protein complex responsible for phosphorolytic degradation and tailing of RNA, has an RNA-binding platform containing Rrp4, Csl4, and DnaG. Aiming to detect novel interaction partners of the exosome, we copurified Nop5, which is a part of an rRNA methylating ribonucleoprotein complex, with the exosome of Sulfolobus solfataricus grown to a late stationary phase. We demonstrated the capability of Nop5 to bind to the exosome with a homotrimeric Rrp4-cap and to increase the proportion of polyadenylated RNAin vitro, suggesting that Nop5 is a dual-function protein. Since tailing of RNA probably serves to enhance RNA degradation, association of Nop5 with the archaeal exosome in the stationary phase may enhance tailing and degradation of RNA as survival strategy.

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The Archaeal Exosome: Identification and Quantification of Site‐Specific Motions That Correlate with Cap and RNA Binding

et al. 2013

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Groß und unerwartet flexibel: Der 173‐kDa‐Exosomkernkomplex erweist sich in Lösung als unerwartet dynamisch. Die kinetischen und thermodynamischen Daten des identifizierten Austauschprozesses wuerden bestimmt. Die Bindung eines Cap‐Proteins wie auch die eines RNA‐Substrats verändern die Bewegungen deutlich, was dafür spricht, dass diese Wechselwirkungen mit der Auswahl einer bestimmten Exosomkonformation (Zustand A im Energiediagramm) einhergehen.

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Heterogeneous complexes of the RNA exosome in Sulfolobus solfataricus

Cited by 24 publications

References 47 publications

A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

A Prototypic Lysine Methyltransferase 4 from Archaea with Degenerate Sequence Specificity Methylates Chromatin Proteins Sul7d and Cren7 in Different Patterns

Nop5 interacts with the archaeal RNA exosome

The Archaeal Exosome: Identification and Quantification of Site‐Specific Motions That Correlate with Cap and RNA Binding

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