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

AUTOR(ES)

Gay, D A

RESUMO

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 cotranslational 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.

Documentos Relacionados

• Physical evidence for cotranslational regulation of beta-tubulin mRNA degradation.
• Regulation of tubulin and actin mRNA production in rat brain: expression of a new beta-tubulin mRNA with development.
• Assembly properties of altered beta-tubulin polypeptides containing disrupted autoregulatory domains.
• Regulation of three beta-tubulin mRNAs during rat brain development.
• Identification of two human beta-tubulin isotypes.