Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use

Atkins, John F.; Loughran, Gary; Bhatt, Pramod R.; Firth, Andrew E.; Baranov, Pavel V.

Mammalian antizyme 1 binds to ATP citrate lyase that catalyzes the synthesis of acetyl-CoA which is involved in lipid anabolism and also in acetylation of cellular proteins. Instead of accelerating ATP citrate lyase degradation, antizyme performs an activating role. Cellular spermidine and spermine induce spermidine/spermine-N 1 -acetyltransferase which acetylates polyamines for catabolism or secretion. A regulatory circuit involving its substrate acetyl-CoA in downregulating spermidine and spermine through acetylation has been proposed. An influence on acetyl-CoA has wider implications, including for histone acetylation, and initial studies on cholesterol have been performed (287) . Antizyme has also been reported to bind to Smad1, cyclin D1 and Aurora-A (288) (289) (290) , though there has been some controversy about this. A study of the binding sites of antizyme and cyclin D1 also revealed that binding affinity was 4-fold lower than for antizyme and ornithine decarboxylase (291) for which high resolution structural information is now available (276) .