Navigation ▼

Show simple item record

dc.contributor.advisor Schwappach, Blanche Prof. Dr.
dc.contributor.author Schaefer, Moritz
dc.date.accessioned 2017-05-17T09:00:28Z
dc.date.available 2017-06-06T22:50:08Z
dc.date.issued 2017-05-17
dc.identifier.uri http://hdl.handle.net/11858/00-1735-0000-0023-3E49-D
dc.language.iso eng de
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc 610 de
dc.title Cysteine residues of the mammalian GET receptor: Essential for tail-anchored protein insertion? de
dc.type doctoralThesis de
dc.contributor.referee Thumm, Michael Prof. Dr.
dc.date.examination 2017-05-30
dc.description.abstracteng Tail-anchored proteins integrate into lipid bilayers via a single transmembrane segment at their extreme C-terminus. The membrane insertion step is mediated by a heterodimeric receptor complex formed by WRB and CAML in higher eukaryotes and Get1 and Get2 in yeast. The transmembrane domains of the receptor complex form an integration site at the endoplasmic reticulum membrane and interact transiently with the transmembrane domain of an integrating TA protein prior to its membrane embedding. Cysteine residues are absent in yeast Get1 and Get2 whereas the mammalian homologues WRB and CAML contain three and five cysteines respectively. I aimed to investigate the role of the cysteine residues of WRB and CAML and test whether they are essential for TA protein targeting. Mutants of WRB and CAML in which the cysteine residues were mutated to serine were generated and I used a yeast-based complementation assay in which cells depleted of Get1 and Get2 were transformed with plasmids encoding either wild type or mutant WRB and CAML. Mutants were still able to create a receptor complex as assayed by yeast two-hybrid and did not impair the targeting of a substrate TA protein. Moreover, mutants rescued growth phenotypes of GET mutants confirming the formation of a functionally active receptor. In line with the absence of cysteines in the yeast GET receptor, cysteines in WRB and CAML seem to be not essential for TA protein targeting and may be required for potential still unknown regulation of TA protein targeting such as receptor stoichiometry, substrate quality control and chaperone function. de
dc.contributor.coReferee Oppermann, Martin Prof. Dr.
dc.subject.eng GET de
dc.subject.eng Guided entry of tail-anchored proteins de
dc.subject.eng WRB de
dc.subject.eng CAML de
dc.subject.eng GET receptor de
dc.subject.eng Yeast two-hybrid de
dc.subject.eng redox regulation de
dc.subject.eng oxidative stress de
dc.identifier.urn urn:nbn:de:gbv:7-11858/00-1735-0000-0023-3E49-D-5
dc.affiliation.institute Medizinische Fakultät de
dc.subject.gokfull Medizin (PPN619874732) de
dc.subject.gokfull Physiologische Chemie de
dc.subject.gokfull Biochemie de
dc.subject.gokfull Pathobiochemie - Allgemein- und Gesamtdarstellungen de
dc.description.embargoed 2017-06-06
dc.identifier.ppn 887658504

Files in this item

This item appears in the following Collection(s)

Show simple item record