| Title | Effects of Thiamine Pyrophosphate on the Inhibition of Self-splicing of Primary Transcripts of T4 phage Thymidylate Synthase Gene in the Presence of GTP |
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| Author | Hyun Joo Lee 1 , Sung Joon Ahn 1 , Sook Shin 2 , and In Kook Park 1 * |
| Address | 1 Department of Biology, Dongguk University, Seoul 100-715, Korea; 2 Department of Biology, Sahmyook University, Seoul 139-742, Korea |
| Bibliography | Journal of Microbiology, 40(2),134-139, 2002, |
| DOI | |
| Key Words | T4 phage, group 1 intron, thiamine pyrophosphate, GTP, self-splicing |
| Abstract | Effects of GTP on the inhibition of self-splicing of primary transcripts of the phage T4 thymidylate synthase gene (td) by thiamine pyrophosphate and its analogs have been investigated. The order of the inhibitory efficiency for compounds tested was as follows: thiamine pyrophosphate > thiamine mono-phosphate > thiamine. Of all compounds examined, thiamine pyrophosphate was the most potent inhibitor. Increasing GTP concentration in splicing reaction tended to overcome the suppressive effects of self-splicing by thiamine pyrophosphate and its analogs. The inhibition by thiamine pyrophosphate was most sensitized to a higher concentration of GTP. It has been speculated that the key structural features in thiamine pyrophosphate and its analogs responsible for the inhibition of splicing may be a thiamine moiety in which the phosphorylation of 2-hydroxylethyl group on 5-position of thiazolium ring rendered further stimulation of inhibition in self-splicing reaction. |
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