RNA molecules stimulate prion protein conversion

Nature

Volumn 425, Issue 6959, 2003, Pages 717-720

  Deleault, Nathan R ^a   Lucassen, Ralf W ^a   Supattapone, Surachai ^a  

^a DARTMOUTH MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CONFORMATIONS; ENZYMES; PROTEINS;

PRION PROTEIN CONVERSION;

RNA;

APYRASE; CYCLIC GMP; CYTIDINE PHOSPHATE; DEOXYRIBONUCLEASE; DOUBLE STRANDED RNA; GLYCOPROTEIN; MICROCOCCAL NUCLEASE; PRION PROTEIN; RIBONUCLEASE; RNA;

ANIMAL TISSUE; ARTICLE; BRAIN HOMOGENATE; CAENORHABDITIS ELEGANS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; ESCHERICHIA COLI; FEMALE; GENE AMPLIFICATION; HAMSTER; IN VITRO STUDY; INVERTEBRATE; MOUSE; NONHUMAN; PATHOGENESIS; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; SACCHAROMYCES CEREVISIAE; STOICHIOMETRY;

ANIMALS; BRAIN; CAENORHABDITIS ELEGANS; CRICETINAE; DROSOPHILA MELANOGASTER; ENDONUCLEASES; ESCHERICHIA COLI; FEMALE; MESOCRICETUS; MICE; PRION DISEASES; PRIONS; PROTEIN CONFORMATION; PROTEIN FOLDING; RNA; SACCHAROMYCES CEREVISIAE; SCRAPIE; SPECIES SPECIFICITY;

ANIMALIA; CAENORHABDITIS; CAENORHABDITIS ELEGANS; CRICETINAE; DROSOPHILA MELANOGASTER; ESCHERICHIA COLI; INVERTEBRATA; MAMMALIA; MELANOGASTER; SACCHAROMYCES; SACCHAROMYCES CEREVISIAE;

EID: 0142184333     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature01979     Document Type: Article

References (16)

1. Prusiner, S. B. Novel proteinaceous infectious particles cause scrapie. Science 216, 136-144 (1982).
2. Prusiner, S. B. (ed.) Prion Biology and Diseases (Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, 1999).
3. Lucassen, R., Nishina, K. & Supattapone, S. In vitro amplification of protease-resistant prion protein requires free sulfhydryl groups. Biochemistry 42, 4127-4135 (2003).
4. Saborio, G. P., Permanne, B. & Soto, C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411, 810-813 (2001).
5. Lockard, R. E. & Kumar, A. Mapping tRNA structure in solution using double-strand-specific ribonuclease VI from cobra venom. Nucleic Acids Res. 9, 5125-5140 (1981).
6. Banks, G. R. A ribonuclease H from Ustilago maydis. Properties, mode of action and substrate specificity of the enzyme. Eur. J. Biochem. 47, 499-507 (1974).
7. Kocisko, D. A. et al. Cell-free formation of protease-resistant prion protein. Nature 370, 471-474 (1994).
8. Caughey, B., Horiuchi, M., Demaimay, R. & Raymond, G. J. Assays of protease-resistant prion protein and its formation. Methods Enzymol. 309, 122-133 (1999).
9. Derrington, E. et al. PrPC has nucleic acid chaperoning properties similar to the nucleocapsid protein of HIV-1. C. R. Acad. Sci. III 325, 17-23 (2002).
10. Moscardini, M. et al. Functional interactions of nucleocapsid protein of feline immunodeficiency virus and cellular prion protein with the viral RNA. J. Mol. Biol. 318, 149-159 (2002).
11. Gabus, C. et al. The prion protein has RNA binding and chaperoning properties characteristic of nucleocapsid protein NCP7 of HIV-1. J. Biol. Chem. 276, 19301-19309 (2001).
12. Gabus, C. et al. The prion protein has DNA strand transfer properties similar to retroviral nucleocapsid protein. J. Mol. Biol. 307, 1011-1021 (2001).
13. Nandi, P. K., Leclerc, E., Nicole, J. C. & Takahashi, M. DNA-induced partial unfolding of prion protein leads to its polymerisation to amyloid. J. Mol. Biol. 322, 153-161 (2002).
14. Cordeiro, Y. et al. DNA converts cellular prion protein into the β-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 276, 49400-49409 (2001).
15. Weissmann, C. A 'unified theory' of prion propagation. Nature 352, 679-683 (1991).
16. Chapon, C., Cech, T. R. & Zaug, A. J. Polyadenylation of telomerase RNA in budding yeast. RNA 3, 1337-1351 (1997).