HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Naito, S. Articles by Ishihama, A. Search for Related Content PubMed PubMed Citation Articles by Naito, S. Articles by Ishihama, A. Social Bookmarking                      What's this?

JBC, Vol. 251, Issue 14, 4307-4314, Jul, 1976

Function and structure of RNA polymerase from vesicular stomatitis virus

S. Naito and A. Ishihama

The RNA-dependent RNA polymerase associated with vesicular stomatitis virus was isolated to apparent homogeneity by a newly developed procedure, which includes stepwise removal of proteins from virions by successive treatment with high concentrations of cesium sulfate and cesium chloride, followed by glycerol gradient centrifugation or chromatography on phosphocellulose or DEAE-Sephadex column. The polymerase thus purified contained L (large protein) and NS proteins as the intrinsic subunits and multiple species of enzyme were found which differ in the molar ratio of L to NS. Since the enzyme with the highest activity was composed of equimolar amounts of the two subunits and exhibited the sedimentation coefficient of approximately 11 S in a buffer containing 0.2 M NaCl, the structure of active protomer was suggested to be (L)1(NS)1. In accordance with this conclusion, enzyme preparations deficient in the content of NS protein, were activated by the addition of preparations deficient in the content of NS protein. The purified RNA polymerase catalyzed the synthesis of poly(A), which was covalently attached to the 3' termini of RNA products, and RNA, only in the presence of all 4 substrates. The present finding might be the first which indicates that the transcriptase itself catalyzes post-transcriptional modification of mRNA by adding poly(A) sequences to the 3'-OH termini. The molecular mechanism of the switch from transcription to poly(A) synthesis, however, remains to be investigated.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. Chen, T. Ogino, and A. K. Banerjee Mapping and Functional Role of the Self-Association Domain of Vesicular Stomatitis Virus Phosphoprotein J. Virol., October 1, 2006; 80(19): 9511 - 9518. [Abstract] [Full Text] [PDF]

				T. J. Green, X. Zhang, G. W. Wertz, and M. Luo Structure of the Vesicular Stomatitis Virus Nucleoprotein-RNA Complex Science, July 21, 2006; 313(5785): 357 - 360. [Abstract] [Full Text] [PDF]

				T. Li and A. K. Pattnaik Overlapping Signals for Transcription and Replication at the 3' Terminus of the Vesicular Stomatitis Virus Genome J. Virol., January 1, 1999; 73(1): 444 - 452. [Abstract] [Full Text] [PDF]

				L. N. Hwang, N. Englund, and A. K. Pattnaik Polyadenylation of Vesicular Stomatitis Virus mRNA Dictates Efficient Transcription Termination at the Intercistronic Gene Junctions J. Virol., March 1, 1998; 72(3): 1805 - 1813. [Abstract] [Full Text] [PDF]

				A. Honda, A. Endo, K. Mizumoto, and A. Ishihama Differential Roles of Viral RNA and cRNA in Functional Modulation of the Influenza Virus RNA Polymerase J. Biol. Chem., August 10, 2001; 276(33): 31179 - 31185. [Abstract] [Full Text] [PDF]