Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli
| العنوان: | Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli |
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| المؤلفون: | Elfageih, Rageia, Karyolaimos, Alexandros, Kemp, Grant, de Gier, Jan-Willem, von Heijne, Gunnar, Kudva, Renuka |
| المصدر: | Protein Science. 29(10):2028-2037 |
| مصطلحات موضوعية: | alkaline phosphatase, disulfide bonds, force profile analysis, periplasm, protein folding |
| الوصف: | Cotranslational protein folding studies using Force Profile Analysis, a method where the SecM translational arrest peptide is used to detect folding-induced forces acting on the nascent polypeptide, have so far been limited mainly to small domains of cytosolic proteins that fold in close proximity to the translating ribosome. In this study, we investigate the cotranslational folding of the periplasmic, disulfide bond-containing Escherichia coli protein alkaline phosphatase (PhoA) in a wild-type strain background and a strain background devoid of the periplasmic thiol: disulfide interchange protein DsbA. We find that folding-induced forces can be transmitted via the nascent chain from the periplasm to the polypeptide transferase center in the ribosome, a distance of similar to 160 angstrom, and that PhoA appears to fold cotranslationally via at least two disulfide-stabilized folding intermediates. Thus, Force Profile Analysis can be used to study cotranslational folding of proteins in an extra-cytosolic compartment, like the periplasm. |
| وصف الملف: | |
| URL الوصول: | https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-185318 https://doi.org/10.1002/pro.3927 |
| قاعدة البيانات: | SwePub |
| تدمد: | 09618368 1469896X |
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| DOI: | 10.1002/pro.3927 |