@article{mbs:/content/journal/jgv/10.1099/0022-1317-70-3-535, author = "Hunt, D. Margaret", title = "Effect of Analogues of S-Adenosylmethionine on in vitro Polyadenylation by Vesicular Stomatitis Virus", journal= "Journal of General Virology", year = "1989", volume = "70", number = "3", pages = "535-542", doi = "https://doi.org/10.1099/0022-1317-70-3-535", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-70-3-535", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "polyadenylation", keywords = "S-adenosylmethionine", keywords = "VSV", abstract = "SUMMARY 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.", }