Unstructured 5'-tails act through ribosome standby to override inhibitory structure at ribosome binding sites.

ABSTRACT: Initiation is the rate-limiting step in translation. It is well-known that stable structure at a ribosome binding site (RBS) impedes initiation. The ribosome standby model of de Smit and van Duin, based on studies of the MS2 phage coat cistron, proposed how high translation rates can be reconciled with stable, inhibitory structures at an RBS. Here, we revisited the coat protein system and assessed the translation efficiency from its sequestered RBS by introducing standby mutations. Further experiments with gfp reporter constructs assessed the effects of 5'-tails-as standby sites-with respect to length and sequence contributions. In particular, combining in vivo and in vitro assays, we can show that tails of CA-dinucleotide repeats-and to a lesser extent, AU-repeats-dramatically increase tr

SUBMITTER: Sterk M 

PROVIDER: S-EPMC5934652 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature