The Dynamics of SecM-Induced Translational Stalling
作者： Albert Tsai , Guy Kornberg , Magnus Johansson , Jin Chen , Joseph D Puglisi
DOI: 10.1016/J.CELREP.2014.04.033
关键词:
摘要: SecM is an E. coli secretion monitor capable of stalling translation on the prokaryotic ribosome without cofactors. Biochemical and structural studies have demonstrated that nascent chain interacts with 50S subunit exit tunnel to inhibit peptide bond formation. However, timescales pathways of stalling mRNA remain undefined. To provide a dynamic mechanism for stalling, we directly tracked dynamics elongation ribosomes translating stall sequence (FSTPVWISQAQGIRAGP) using single-molecule fluorescence techniques. Within 1 min, three peptide-ribosome interactions work cooperatively over last five codons sequence, leading severely impaired rates beginning from terminal proline lasting four codons. Our results suggest tightly linked underscore roles play in controlling fundamental steps translation.
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