Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins
Abstract The membrane insertase YidC inserts newly synthesized proteins by its hydrophobic slide consisting of the two transmembrane (TM) segments TM3 and TM5. Mutations in this part of the protein affect the insertion of the client proteins. We show here that a quintuple mutation, termed YidC-5S, i...
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2021
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oai:doaj.org-article:cdbe565b07bf43628edf13ae8296fd9e2021-12-02T12:11:17ZMolecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins10.1038/s41598-021-83224-x2045-2322https://doaj.org/article/cdbe565b07bf43628edf13ae8296fd9e2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83224-xhttps://doaj.org/toc/2045-2322Abstract The membrane insertase YidC inserts newly synthesized proteins by its hydrophobic slide consisting of the two transmembrane (TM) segments TM3 and TM5. Mutations in this part of the protein affect the insertion of the client proteins. We show here that a quintuple mutation, termed YidC-5S, inhibits the insertion of the subunit a of the FoF1 ATP synthase but has no effect on the insertion of the Sec-independent M13 procoat protein and the C-tail protein SciP. Further investigations show that the interaction of YidC-5S with SecY is inhibited. The purified and fluorescently labeled YidC-5S did not approach SecYEG when both were co-reconstituted in proteoliposomes in contrast to the co-reconstituted YidC wild type. These results suggest that TM3 and TM5 are involved in the formation of a common YidC-SecYEG complex that is required for the insertion of Sec/YidC-dependent client proteins.Anja SteudleDirk SpannEva ProssSri Karthika ShanmugamRoss E. DalbeyAndreas KuhnNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021) |
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Medicine R Science Q Anja Steudle Dirk Spann Eva Pross Sri Karthika Shanmugam Ross E. Dalbey Andreas Kuhn Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins |
description |
Abstract The membrane insertase YidC inserts newly synthesized proteins by its hydrophobic slide consisting of the two transmembrane (TM) segments TM3 and TM5. Mutations in this part of the protein affect the insertion of the client proteins. We show here that a quintuple mutation, termed YidC-5S, inhibits the insertion of the subunit a of the FoF1 ATP synthase but has no effect on the insertion of the Sec-independent M13 procoat protein and the C-tail protein SciP. Further investigations show that the interaction of YidC-5S with SecY is inhibited. The purified and fluorescently labeled YidC-5S did not approach SecYEG when both were co-reconstituted in proteoliposomes in contrast to the co-reconstituted YidC wild type. These results suggest that TM3 and TM5 are involved in the formation of a common YidC-SecYEG complex that is required for the insertion of Sec/YidC-dependent client proteins. |
format |
article |
author |
Anja Steudle Dirk Spann Eva Pross Sri Karthika Shanmugam Ross E. Dalbey Andreas Kuhn |
author_facet |
Anja Steudle Dirk Spann Eva Pross Sri Karthika Shanmugam Ross E. Dalbey Andreas Kuhn |
author_sort |
Anja Steudle |
title |
Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins |
title_short |
Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins |
title_full |
Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins |
title_fullStr |
Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins |
title_full_unstemmed |
Molecular communication of the membrane insertase YidC with translocase SecYEG affects client proteins |
title_sort |
molecular communication of the membrane insertase yidc with translocase secyeg affects client proteins |
publisher |
Nature Portfolio |
publishDate |
2021 |
url |
https://doaj.org/article/cdbe565b07bf43628edf13ae8296fd9e |
work_keys_str_mv |
AT anjasteudle molecularcommunicationofthemembraneinsertaseyidcwithtranslocasesecyegaffectsclientproteins AT dirkspann molecularcommunicationofthemembraneinsertaseyidcwithtranslocasesecyegaffectsclientproteins AT evapross molecularcommunicationofthemembraneinsertaseyidcwithtranslocasesecyegaffectsclientproteins AT srikarthikashanmugam molecularcommunicationofthemembraneinsertaseyidcwithtranslocasesecyegaffectsclientproteins AT rossedalbey molecularcommunicationofthemembraneinsertaseyidcwithtranslocasesecyegaffectsclientproteins AT andreaskuhn molecularcommunicationofthemembraneinsertaseyidcwithtranslocasesecyegaffectsclientproteins |
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1718394658074132480 |