Abstract
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 doughnut-shaped 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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Acknowledgments
The authors would like to thank Drs H Wilson and SN Cohen for their critical reading and comments on the manuscript. Work in S L-C lab was supported by grants from the National Science Council, ROC (95-2311-B-001-055 & -034), an Academia Sinica Institutional Research grant, and a JCEF research fund. Work in GS lab was supported by grants from Israel Science Foundation (ISF), United States-Israel Binational Science Foundation (BSF) and the United States-Israel Binational Agricultural Research and Development Fund (BARD).
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Lin-Chao, S., Chiou, NT. & Schuster, G. The PNPase, exosome and RNA helicases as the building components of evolutionarily-conserved RNA degradation machines. J Biomed Sci 14, 523–532 (2007). https://doi.org/10.1007/s11373-007-9178-y
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DOI: https://doi.org/10.1007/s11373-007-9178-y