PMID: 9448684Feb 4, 1998Paper

Amino terminus of reovirus nonstructural protein sigma NS is important for ssRNA binding and nucleoprotein complex formation

Virology
A L Gillian, M L Nibert

Abstract

Reovirus nonstructural protein sigma NS exhibits a ssRNA-binding activity thought to be involved in assembling the reovirus mRNAs for genome replication and virion morphogenesis. To extend analysis of this activity, recombinant sigma NS (r sigma NS) was expressed in insect cells using a recombinant baculovirus. In infected-cell extracts, r sigma NS was found in large complexes (> or = 30 S) that were disassembled into smaller, 13-19 S complexes upon treatment with RNase A. R sigma NS also bound to poly(A)-Sepharose beads both before and after purification. Treatment with high salt during purification caused r sigma NS to sediment in even smaller, 7-9 S complexes, consistent with more complete loss of RNA. To localize the RNA-binding site, limited proteolysis was used to fragment the r sigma NS protein. Upon mild treatment with thermolysin, 11 amino acids were removed from the amino terminus of r sigma NS, and the resulting protein no longer bound to poly(A). In addition, when r sigma NS in cell extracts was treated with thermolysin to generate the amino-terminally truncated from, it sedimented at 7-9 S, also consistent with the loss of RNA-binding capacity. To confirm these findings, a deletion mutant lacking amino acids 2-11 w...Continue Reading

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Citations

Aug 31, 2006·Journal of Virology·Takeshi KobayashiTerence S Dermody
Jan 24, 2007·BMC Molecular Biology·Alak Kanti KarPolly Roy
Mar 11, 2004·Virus Research·Hariharan JayaramB V Venkataram Prasad
Jan 9, 2016·Veterinary Research·Hanne Merethe HaatveitEspen Rimstad
Jun 26, 2015·Nucleic Acids Research·Alexander BorodavkaRoman Tuma
Jan 1, 2014·Uirusu·Takeshi Kobayashi
Mar 3, 2004·The Journal of General Virology·Catherine EichwaldOscar R Burrone
Mar 24, 2005·The Journal of General Virology·Fernando Tourís-OteroJavier Benavente

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