| Literature DB >> 14592411 |
Tomoaki Ogino1, Minako Iwama, Yuki Ohsawa, Kiyohisa Mizumoto.
Abstract
Cellular tubulin has been shown to activate in vitro transcription with Sendai virus (SeV) particles. In this study, the molecular basis for the transcriptional activation by tubulin was investigated. We showed that tubulin dissociates viral matrix (M) protein, which acts as a negative regulator for transcription, from viral ribonucleoprotein (RNP) consisting of L, P, N proteins, and the genome RNA. Both alpha and beta subunits of human tubulin, which were expressed as GST fusion proteins, were found to stimulate viral mRNA synthesis similar to native alpha/beta-heterodimer tubulin. Pull-down assay using GST-tubulin subunits demonstrated that M protein is released from the RNP as a complex with each tubulin subunit. In vitro-binding analyses revealed that M protein directly interacts with tubulin as well as microtubules. These findings suggest that interaction of M protein with tubulin may have an important role in the regulation of SeV transcription.Entities:
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Year: 2003 PMID: 14592411 DOI: 10.1016/j.bbrc.2003.09.205
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575