Document Detail

Prion and anti-codon usage: does infectious PrP alter tRNA abundance to induce misfolding of PrP?
MedLine Citation:
PMID:  18809261     Owner:  NLM     Status:  MEDLINE    
The "protein-only" hypothesis of prion diseases views the infectious agent as devoid of nucleic acids and consisting of misfolded prion proteins (PrP(Sc)) which, upon infiltration into host cells, act as a template that induces transformation of wild-type protein (PrP(C)) to the pathological form by unknown mechanisms. The two isoforms are identical in amino-acid composition. By analogy to reported "silent" mutations in which utilization of relatively rare tRNAs alter protein folding pattern, we postulate that misfolded PrP(Sc) alters tRNAs abundance in prion-infected cells and results in different rates of co-translational folding of PrP, leading to the formation of additional misfolded PrP(Sc). We analyze experiments that might link tRNAs to prions. This concept of "PrP-seed and tRNA-soil" envisages a vicious cycle in which PrP(Sc) levels govern specific tRNA usage, whose alteration subsequently transforms resident PrP(C) to PrP(Sc), causing the cycle to repeat itself ad infinitum.
Oded Rechavi; Yoel Kloog
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-09-21
Journal Detail:
Title:  Medical hypotheses     Volume:  72     ISSN:  0306-9877     ISO Abbreviation:  Med. Hypotheses     Publication Date:  2009 Feb 
Date Detail:
Created Date:  2008-12-29     Completed Date:  2009-03-31     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7505668     Medline TA:  Med Hypotheses     Country:  Scotland    
Other Details:
Languages:  eng     Pagination:  193-5     Citation Subset:  IM    
Department of Neurobiology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, 69978 Tel-Aviv, Israel.
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MeSH Terms
Codon / genetics*
Prions / genetics*
Protein Folding*
RNA, Transfer / genetics*
Reg. No./Substance:
0/Codon; 0/Prions; 9014-25-9/RNA, Transfer

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