TY  - JOUR
AU  - Marbach, Jendrik
AU  - Zentis, Peter
AU  - Ellinger, Philipp
AU  - Müller, Henrik
AU  - Birkmann, Eva
TI  - Expression and characterisation of fully posttranslationally modified cellular prion protein in Pichia pastoris
JO  - Biological chemistry
VL  - 394
IS  - 11
SN  - 1437-4315
CY  - Berlin [u.a.]
PB  - de Gruyter
M1  - FZJ-2014-00278
SP  - 1475-1483
PY  - 2013
AB  - Prion diseases are fatal neurodegenerative diseases which occur as sporadic, genetic, and transmissible disorders. A molecular hallmark of prion diseases is the conformational conversion of the host-encoded cellular form of the prion protein (PrPC) into its misfolded pathogenic isoform (PrPSc). PrPSc is the main component of the pathological and infectious prion agent. The study of the conversion mechanism from PrPC to PrPSc is a major field in prion research. PrPC is glycosylated and attached to the plasma membrane via its glycosyl phosphatidyl inositol (GPI)-anchor. In this study we established and characterised the expression of fully posttranslationally modified mammalian Syrian golden hamster PrPC in the yeast Pichia pastoris using native PrPC-specific N- and C-terminal signal sequences. In vivo as well as in vitro-studies demonstrated that the signal sequences controlled posttranslational processing and trafficking of native PrPC, resulting in PrPC localised in the plasma membrane of P. pastoris. In addition, the glycosylation pattern of native PrPC could be confirmed.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000325717100011
DO  - DOI:10.1515/hsz-2013-0180
UR  - https://juser.fz-juelich.de/record/150199
ER  -