Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene.
PrP 27-30 is the major protein in purified preparations of scrapie agent. An almost complete PrP cDNA was used to select PrP-related genomic clones from normal hamster DNA. The gene contains a noncoding exon of 56 to 82 bp and a 2 kb coding exon, separated by a 10 kb intron. Transcription initiates at the same multiple sites in vivo and in vitro. The promoter lacks a TATA box and contains three repeats of the sequence GCCCCGCCC, which resembles the Sp1 binding site found in "housekeeping" genes. The PrP coding sequence encodes a presumptive amino-terminal signal peptide. The primary structure of PrP encoded by the gene of a healthy animal does not differ from that encoded by a cDNA from a scrapie-infected animal, suggesting that the different properties of PrP from normal and scrapie-infected brains are due to post-translational events.
Basler
K
K
Oesch
B
B
Scott
M
M
Westaway
D
D
Wälchli
M
M
Groth
D F
DF
McKinley
M P
MP
Prusiner
S B
SB
Weissmann
C
C
D000818:Animals; D001483:Base Sequence; D001923:Brain Chemistry; D006224:Cricetinae / Q000235:genetics*; D004247:DNA / Q000032:analysis; D008647:Mesocricetus / Q000235:genetics*; D011061:Poly A / Q000235:genetics; D018622:PrP 27-30 Protein; D011328:Prions / Q000235:genetics*; D011401:Promoter Regions, Genetic; D011498:Protein Precursors / Q000096:biosynthesis; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000235:genetics; D012333:RNA, Messenger / Q000235:genetics; D014764:Viral Proteins / Q000096:biosynthesis
D011328:Prions; D011498:Protein Precursors; D021382:Protein Sorting Signals; D012333:RNA, Messenger; D014764:Viral Proteins; D018622:PrP 27-30 Protein; D011061:Poly A; D004247:DNA