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Effect of Analogues of S-Adenosylmethionine on in vitro Polyadenylation by Vesicular Stomatitis Virus

Department of Microbiology and Immunology, University of South Carolina School of Medicine, Columbia, South Carolina 29208, U.S.A.

Other workers have reported that vesicular stomatitis virus makes aberrantly long polyadenylic acid [poly(A)] tracts in the presence of S-adenosylhomocysteine (S-Ado-Hcy). In the work reported in this paper, the effects of various analogues of S-adenosylmethionine (S-Ado-Met) and ATP on polyadenylation in an in vitro transcription system were examined to determine whether S-Ado-Hcy exerted its effect on polyadenylation due to its relationship to S-Ado-Met or to ATP. It appeared that compounds which affected polyadenylation were those which were closely related to S-Ado-Met and that had the same L-aminoacyl side chain [(COOH)-CH(NH)₂-CH₂-CH₂-]; the nature of the substituent at the -S⁺(CH₃)- position of S-Ado-Met was less important. These analogues appeared to compete with S-Ado-Met for a binding site(s). These data support a model whereby compounds binding at an S-Ado-Met-binding site may have allosteric effects by causing or preventing conformational changes which are involved in polyadenylation reactions, perhaps by affecting the rate of polyadenylation or of termination.

Keywords: VSV, S-adenosylmethionine, polyadenylation

Received 2 September 1988; accepted 9 November 1988.

This article has been cited by other articles:

				S. E. Galloway and G. W. Wertz S-Adenosyl Homocysteine-Induced Hyperpolyadenylation of Vesicular Stomatitis Virus mRNA Requires the Methyltransferase Activity of L Protein J. Virol., December 15, 2008; 82(24): 12280 - 12290. [Abstract] [Full Text] [PDF]

				E. A. Stillman and M. A. Whitt Transcript Initiation and 5'-End Modifications Are Separable Events during Vesicular Stomatitis Virus Transcription J. Virol., September 1, 1999; 73(9): 7199 - 7209. [Abstract] [Full Text]