The dynamics of SecM-induced translational stalling

Albert Tsai, Guy Kornberg, Magnus Johansson, Jin Chen, Joseph D. Puglisi

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

SecM is an E. coli secretion monitor capable ofstalling translation on the prokaryotic ribosome without cofactors. Biochemical and structural studies have demonstrated that the SecM nascent chain interacts with the 50S subunit exit tunnel to inhibit peptide bond formation. However, the timescales and pathways of stalling on an mRNA remain undefined. To provide a dynamic mechanism for stalling, we directly tracked the dynamics of elongation on ribosomes translating the SecM stall sequence (FSTPVWISQAQGIRAGP) using single-molecule fluorescence techniques. Within 1min, three peptide-ribosome interactions work cooperatively over the last five codons of the SecM sequence, leading to severely impaired elongation rates beginning from the terminal proline and lasting four codons. Our results suggest that stalling is tightly linked to the dynamics of elongation and underscore the roles that the exit tunnel and nascent chain play in controlling fundamental steps in translation.

Original languageEnglish (US)
Pages (from-to)1521-1533
Number of pages13
JournalCell Reports
Volume7
Issue number5
DOIs
StatePublished - Jun 12 2014
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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