An exosome‐like complex in <i>Sulfolobus solfataricus</i>

Evguenieva‐Hackenberg, Elena; Walter, Pamela; Hochleitner, Elisabeth O.; Lottspeich, Friedrich; Klug, Gabriele

doi:10.1038/sj.embor.embor929

Cited by 130 publications

(139 citation statements)

References 21 publications

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“…Most Archaea harbor a similar complex named the archaeal exosome [2,3]. The structure of this complex is similar to the structures of the nine-subunit core of the eukaryotic exosome and of the bacterial polynucleotide phosphorylase (PNPase) ( Supplementary Fig.…”

Section: Introductionmentioning

confidence: 72%

The evolutionarily conserved subunits Rrp4 and Csl4 confer different substrate specificities to the archaeal exosome

Roppelt

Klug

Evguenieva‐Hackenberg

2010

FEBS Letters

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a b s t r a c tWe studied the substrate specificity of the exosome of Sulfolobus solfataricus using the catalytically active Rrp41-Rrp42-hexamer and complexes containing the RNA-binding subunits Rrp4 or Csl4. The conservation of both Rrp4 and Csl4 in archaeal and eukaryotic exosomes suggests specific functions for each of them. We found that they confer different specificities to the exosome: RNA with an Apoor 3 0 -end is degraded with higher efficiency by the Csl4-exosome, while the Rrp4-exosome strongly prefers poly(A)-RNA. High C-content and polyuridylation negatively influence RNA processing by all complexes, and, in contrast to the hexamer, the Rrp4-exosome prefers longer substrates.

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Section: Introductionmentioning

confidence: 72%

The evolutionarily conserved subunits Rrp4 and Csl4 confer different substrate specificities to the archaeal exosome

Roppelt

Klug

Evguenieva‐Hackenberg

2010

FEBS Letters

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“…However, several hyperthermophilic and methanogenic Archaea contain a protein complex that is composed of two proteins (Rrp41 and Rrp42) homologous to RNase PH and one protein containing a KH/S1 domain [33]. Three copies of the three proteins form a nine-subunit complex termed the archaeal exosome that, as with PNPase, is responsible for the polyadenylation and degradation of RNA [29,30,[34][35][36][37].…”

Section: Similar Structure Of the Rnase Ph Pnpase And Exosome Complexesmentioning

confidence: 99%

The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines

2007

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The structure and function of polynucleotide phosphorylase (PNPase) and the exosome, as well as their associated RNA-helicases proteins, are described in the light of recent studies. The picture raised is of an evolutionarily conserved RNA-degradation machine which exonucleolytically degrades RNA from 3¢ to 5¢. In prokaryotes and in eukaryotic organelles, a trimeric complex of PNPase forms a circular doughnutshaped structure, in which the phosphorolysis catalytic sites are buried inside the barrel-shaped complex, while the RNA binding domains create a pore where RNA enters, reminiscent of the protein degrading complex, the proteasome. In some archaea and in the eukaryotes, several different proteins form a similar circle-shaped complex, the exosome, that is responsible for 3¢ to 5¢ exonucleolytic degradation of RNA as part of the processing, quality control, and general RNA degradation process. Both PNPase in prokaryotes and the exosome in eukaryotes are found in association with protein complexes that notably include RNA helicase.

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“…(11) are also shown. For convenience, in the present work we use the nomenclature aRrp4, aRrp41, and aRrp42 for archaeal proteins, as was previously employed (13). H denotes the ␣-helical domain in PNPase.…”

Section: Gel Filtration Analysismentioning

confidence: 99%

“…1A). Recently, a complex containing these proteins was isolated from Sulfolobus solfataricus (13). The coprecipitation of 16 S rRNA and ribosomal proteins with this complex suggests its participation in rRNA processing in Archaea.…”

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confidence: 99%

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The Pyrococcus Exosome Complex

Ramos

Oliveira

Torriani

et al. 2006

Journal of Biological Chemistry

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The exosome is a conserved eukaryotic enzymatic complex that plays an essential role in many pathways of RNA processing and degradation. Here, we describe the structural characterization of the predicted archaeal exosome in solution using small angle x-ray scattering. The structure model calculated from the small angle x-ray scattering pattern provides an indication of the existence of a disk-shaped structure, corresponding to the "RNases PH ring" complex formed by the proteins aRrp41 and aRrp42. The RNases PH ring complex corresponds to the core of the exosome, binds RNA, and has phosphorolytic and polymerization activities. Three additional molecules of the RNA-binding protein aRrp4 are attached to the core as extended and flexible arms that may direct the substrates to the active sites of the exosome. In the presence of aRrp4, the activity of the core complex is enhanced, suggesting a regulatory role for this protein. The results shown here also indicate the participation of the exosome in RNA metabolism in Archaea, as was established in Eukarya.

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An exosome‐like complex in Sulfolobus solfataricus

Cited by 130 publications

References 21 publications

The evolutionarily conserved subunits Rrp4 and Csl4 confer different substrate specificities to the archaeal exosome

The evolutionarily conserved subunits Rrp4 and Csl4 confer different substrate specificities to the archaeal exosome

The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines

The Pyrococcus Exosome Complex

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