Author: Brauburger, Kristina; Hume, Adam J.; Mühlberger, Elke; Olejnik, Judith
Title: Forty-Five Years of Marburg Virus Research Document date: 2012_10_1
ID: 0hlj6r10_52
Snippet: VP35 is a polymerase cofactor and essential for transcription and replication. Together with the catalytic subunit L, VP35 forms the RNA-dependent RNA polymerase complex [134, 143] . VP35 is tightly associated with NP and serves as a bridging protein between the nucleocapsid complex and L. Without VP35, L is not associated with the nucleocapsids which serve as the templates for viral transcription and replication [115, 134] . VP35 forms homo-olig.....
Document: VP35 is a polymerase cofactor and essential for transcription and replication. Together with the catalytic subunit L, VP35 forms the RNA-dependent RNA polymerase complex [134, 143] . VP35 is tightly associated with NP and serves as a bridging protein between the nucleocapsid complex and L. Without VP35, L is not associated with the nucleocapsids which serve as the templates for viral transcription and replication [115, 134] . VP35 forms homo-oligomers mediated by a coiled-coil motif located in the N-terminal part of the protein. Homo-oligomerization of VP35 is essential for its interaction with L but not needed for redistribution of VP35 into NP-derived inclusions [144] . VP35 shares many features with the phospho (P) proteins of other NNS RNA viruses, including its position as the second gene in the viral genome and its role in transcription and replication. However, in contrast to the P proteins, VP35 is either not or only very weakly phosphorylated [145] .
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