|PROSITE documentation PDOC00200 [for PROSITE entry PS00228]|
The stability of β-tubulin mRNAs are autoregulated by their own translation product . Unpolymerized tubulin subunits bind directly (or activate a factor(s) which binds co-translationally) to the nascent N-terminus of β-tubulin. This binding is transduced through the adjacent ribosomes to activate an RNAse that degrades the polysome-bound mRNA. The recognition element has been shown to be the first four amino acids of β-tubulin: Met-Arg-Glu-Ile. Mutations to this sequence abolish the autoregulation effect (except for the replacement of Glu by Asp); transposition of this sequence to an internal region of a polypeptide also suppresses the autoregulatory effect.Last update:
May 1991 / Pattern and text revised.
PROSITE method (with tools and information) covered by this documentation:
|Title||Autoregulated instability of tubulin mRNAs: a novel eukaryotic regulatory mechanism.|
|Source||Trends Biochem. Sci. 13:339-343(1988).|