Autoregulatory control of beta-tubulin mRNA stability is linked to translation elongation.

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Abstract
Tubulin synthesis in animal cells is controlled in part by an autoregulatory mechanism that modulates the stability of ribosome-bound tubulin mRNAs. For .beta. tubulin, the initial recognition event for this selective RNA instability has previously been shown to be a cotraslational binding (presumably by tubulin itself) to the nascent amino-terminal .beta.-tubulin tetrapeptide just after it emerges from the ribosome. Although this "autoregulation" of tubulin expression is thus obligatorily linked to the translation process, the mechanism of how a cotranslational protein-protein binding event ultimately triggers RNA degradation is unknown. Using protein synthesis inhibitors to slow and ultimately to block translation elongation, we now show that the mRNA destabilization pathway requires ongoing ribosome translocation.