An ATPase activity associated with the rotavirus phosphoprotein NSP5

Abstract Interactions between NSP5 and NSP2 drive the formation of viroplasms, sites of genome replication and packaging in rotavirus-infected cells. The serine–threonine-rich NSP5 transitions between hypo- and hyper-phosphorylated isomers during the replication cycle. In this study, we determined t...

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Veröffentlicht in:	Virology (New York, N.Y.) N.Y.), 2007-12, Vol.369 (2), p.389-399
Hauptverfasser:	Bar-Magen, Tamara, Spencer, Eugenio, Patton, John T
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals ATPase Base Sequence Ca(2+) Mg(2+)-ATPase - genetics Ca(2+) Mg(2+)-ATPase - metabolism DNA Primers - genetics DNA, Viral - genetics Humans Infectious Disease Kinetics Molecular Sequence Data Mutagenesis, Site-Directed NSP5 Phosphoprotein Phosphorylation Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Viral - genetics RNA, Viral - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Rotavirus Rotavirus - classification Rotavirus - genetics Rotavirus - metabolism Rotavirus - pathogenicity Sequence Homology, Amino Acid Substrate Specificity Viral Nonstructural Proteins - genetics Viral Nonstructural Proteins - metabolism
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