NDLI: RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 αβγ for its activity

Content Provider	PubMed Central
Author	Das, Tapas Mathur, Manjula Gupta, Ashim K. Janssen, George M. C. Banerjee, Amiya K.
Copyright Year	1998
Abstract	An RNA-dependent RNA polymerase is packaged within the virions of purified vesicular stomatitis virus, a nonsegmented negative-strand RNA virus, which carries out transcription of the genome RNA into mRNAs both in vitro and in vivo. The RNA polymerase is composed of two virally encoded polypeptides: a large protein L (240 kDa) and a phosphoprotein P (29 kDa). Recently, we obtained biologically active L protein from insect cells following infection by a recombinant baculovirus expressing L gene. During purification of the L protein from Sf21 cells, we obtained in addition to an active L fraction an inactive fraction that required uninfected insect cell extract to restore its activity. The cellular factors have now been purified, characterized, and shown to be β and γ subunits of the protein synthesis elongation factor EF-1. We also demonstrate that the α subunit of EF-1 remains tightly bound to the L protein in the inactive fraction and βγ subunits associate with the L(α) complex. Further purification of L(α) from the inactive fraction revealed that the complex is partially active and is significantly stimulated by the addition of βγ subunits purified from Sf21 cells. A putative inhibitor(s) appears to co-elute in the inactive fraction that blocked the L(α) activity. The purified virions also package all three subunits of EF-1. These findings have a striking similarity with Qβ RNA phage, which also associates with the bacterial homologue of EF-1 for its replicase function, implicating a possible evolutionary relationship between these host proteins and the RNA-dependent RNA polymerase of RNA viruses.
Starting Page	1449
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	4
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-02-17
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 alphabetagamma for its activity.

Molecular architecture of the vesicular stomatitis virus RNA polymerase

Translation and identification of the mRNA species synthesized in vitro by the virion-associated RNA polymerase of vesicular stomatitis virus.

Coupled in vitro transcription and translation of vesicular stomatitis virus messenger RNA.

Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase

Sequence-specific contacts between the RNA polymerase of vesicular stomatitis virus and the leader RNA gene.

Ribonucleic Acid Synthesis of Vesicular Stomatitis Virus, II. An RNA Polymerase in the Virion *

In Vitro Synthesis of RNA That Contains Polyadenylate by Virion-Associated RNA Polymerase of Vesicular Stomatitis Virus

Expression of a cDNA encoding a functional 241-kilodalton vesicular stomatitis virus RNA polymerase.

RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 αβγ for its activity

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RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 alphabetagamma for its activity.

Molecular architecture of the vesicular stomatitis virus RNA polymerase

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Histidine-mediated RNA transfer to GDP for unique mRNA capping by vesicular stomatitis virus RNA polymerase

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RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 αβγ for its activity