Effect of analogues of S-adenosylmethionine on in vitro polyadenylation by vesicular stomatitis virus.
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.
Hunt
D M
DM
Department of Microbiology and Immunology, University of South Carolina School of Medicine, Columbia 29208.
D001665:Binding Sites / Q000187:drug effects; D001667:Binding, Competitive / Q000187:drug effects; D011061:Poly A / Q000096:biosynthesis*; D012333:RNA, Messenger / Q000096:biosynthesis*; D012436:S-Adenosylmethionine / Q000031:analogs & derivatives* / Q000494:pharmacology; D013329:Structure-Activity Relationship; D014158:Transcription, Genetic / Q000187:drug effects; D014721:Vesicular stomatitis Indiana virus / Q000187:drug effects* / Q000201:enzymology
D012333:RNA, Messenger; D011061:Poly A; D012436:S-Adenosylmethionine