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Measuring Endoplasmic Reticulum Signal Sequences Translocation Efficiency Using the Xbp1 Arrest Peptide
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Number of Authors: 42018 (English)In: Cell Chemical Biology, ISSN 2451-9456, E-ISSN 2451-9448, Vol. 25, no 7, p. 880-890Article in journal (Refereed) Published
Abstract [en]

Secretory proteins translocate across the mammalian ER membrane co-translationally via the ribosome-sec61 translocation machinery. Signal sequences within the polypeptide, which guide this event, are diverse in their hydrophobicity, charge, length, and amino acid composition. Despite the known sequence diversity in the ER signals, it is generally assumed that they have a dominant role in determining co-translational targeting and translocation process. We have analyzed co-translational events experienced by secretory proteins carrying efficient versus inefficient signal sequencing, using an assay based on Xbp1 peptide-mediated translational arrest. With this method we were able to measure the functional efficiency of ER signal sequences. We show that an efficient signal sequence experiences a two-phase event whereby the nascent chain is pulled from the ribosome during its translocation, thus resuming translation and yielding full-length products. Conversely, the inefficient signal sequence experiences a single weaker pulling event, suggesting inadequate engagement by the translocation machinery of these marginally hydrophobic signal sequences.

Place, publisher, year, edition, pages
2018. Vol. 25, no 7, p. 880-890
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-159061DOI: 10.1016/j.chembiol.2018.04.006ISI: 000439177400010PubMedID: 29754956OAI: oai:DiVA.org:su-159061DiVA, id: diva2:1242443
Available from: 2018-08-28 Created: 2018-08-28 Last updated: 2018-08-28Bibliographically approved

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Kriegler, TheresaMagoulopoulou, AnastasiaMarchal, Rocio AmateHessa, Tara
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