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Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides
Published on: June 19, 2012
Identification of a SecM segment required for export-coupled release from elongation arrest
Kenta Nakamori1, Shinobu Chiba1, Koreaki Ito1
1Faculty of Life Sciences and Structural Biology Research Center, Kyoto Sangyo University, Kyoto 603-8555, Japan.
Abstract:
SecM in Escherichia coli has two functionally crucial regions. The arrest motif near the C-terminus interacts with the ribosomal exit tunnel to arrest its own translational elongation. The signal sequence at the N-terminus directs the SecM nascent polypeptide to the Sec-mediated export pathway to release the arrested state of translation. Here, we addressed the importance of the central region of SecM. Characterization of internal substitution and deletion mutants revealed that a segment from residue 100 to residue 109 is required for the export-coupled release of the SecM nascent chain from the elongation-arrested state. Thus, the central region of SecM is not just a geometric linker but it participates actively in the regulation of translation arrest.
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