NR ASEI
AU Schröder,H.C.; Scheffer,U.; Forrest,J.M.S.; Seve,A.P.; Rytik,P.G.; Müller,W.E.G.
TI Association of scrapie prion protein and prion protein-rna stem-loop with nuclear carbohydrate-binding protein-35 and other rna-binding proteins
QU Neurodegeneration. A Journal for neurodegenerative Disorders, Neuroprotection, and Neuroregeneration 1994 Sep; 3(N3): 177-189
PT Article
AB A number of cellular proteins were identified that bind to the predicted RNA stem-loop structure of prion protein (PrP) RNA; a virtually identical set of RNA-binding proteins was found to associate with the trans-activating region TAR of the human immunodeficiency virus-1. The predicted hairpin elements of the PrP mRNA contain, like TAR RNA, a CUGGG sequence in the loop and a uridine and adenine bulge in the stem; these features are unique among cellular RNAs. UV cross- linking of RNA.protein complexes formed between PrP RNA and HeLa nuclear protein yielded four prominent RNase-resistant complexes, in addition to some minor bands, which migrated at approximate to 90, 68, 42, and 37kDa under denaturing conditions. The presence of multiple PrP RNA-binding, as well as TAR RNA-binding polypeptides was also demonstrated in Northwestern assays with nuclear extracts from mouse ascites, liver, and spleen, whereas only one PrP RNA-binding protein (a doublet with an approximate molecular mass of 35kDa) was found in brain extract from rat. The nuclear beta-galactoside- specific lectin, CBP35 (carbohydrate-binding protein with a molecular mass of 35 kDa), which has been identified in nuclear ribonucleoprotein (RNP) complexes from a variety of mammalian tissues and cells, was among those proteins which bind to PrP RNA. The cellular prion protein, PrPc, was found to be unable to bind PrP RNA directly; however, this protein could be detected in the RNP/CBP35 complex formed between PrP RNA and rat brain extracts. Association of PrPc with RNP/CBP35 complex was abolished by RNase treatment. CBP35 could be also detected in purified infectious scrapie prions, suggesting a possible role in prion replication.
ZR 53
SP englisch
AD H.C. Schröder, Univ Mainz, Inst Physiol Chem, Angew Molek Biol ABT, Duesbergweg 6, D-55099 Mainz, Germany