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Titolo:
Mutation processes at the protein level: is Lamarck back?
Autore:
Chernoff, YO;
Indirizzi:
Georgia Inst Technol, Sch Biol, Atlanta, GA 30332 USA Georgia Inst Technol Atlanta GA USA 30332 Sch Biol, Atlanta, GA 30332 USA
Titolo Testata:
MUTATION RESEARCH-REVIEWS IN MUTATION RESEARCH
fascicolo: 1, volume: 488, anno: 2001,
pagine: 39 - 64
SICI:
1383-5742(200103)488:1<39:MPATPL>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
YEAST SACCHAROMYCES-CEREVISIAE; HEAT-SHOCK-PROTEIN; DE-NOVO APPEARANCE; CHAIN RELEASE FACTORS; PRION-LIKE FACTOR; SUP35 PROTEIN; SPECIES BARRIER; PSI+ PRION; TRANSLATION TERMINATION; IN-VITRO;
Keywords:
prion; amyloid; structural inheritance; chaperone; protein conformation;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
150
Recensione:
Indirizzi per estratti:
Indirizzo: Chernoff, YO Georgia Inst Technol, Sch Biol, M-C 0363,315 Ferst Dr, Atlanta, GA 30332 USA Georgia Inst Technol M-C 0363,315 Ferst Dr Atlanta GA USA 30332
Citazione:
Y.O. Chernoff, "Mutation processes at the protein level: is Lamarck back?", MUT RES-R M, 488(1), 2001, pp. 39-64

Abstract

The experimental evidence accumulated for the last half of the century clearly suggests that inherited variation is not restricted to the changes in genomic sequences. The prion model, originally based on unusual transmission of certain neurodegenerative diseases in mammals, provides a molecular mechanism for the template-like reproduction of alternative protein conformations. Recent data extend this model to protein-based genetic elements in yeast and other fungi. Reproduction and transmission of yeast protein-based genetic elements is controlled by the "prion replication" machinery of the cell, composed of the protein helpers responsible for the processes of assembly and disassembly of protein structures and multiprotein complexes. Amongthese, the stress-related chaperones of Hsp100 and Hsp70 groups play an important role. Alterations of levels or activity of these proteins result in"mutator" or "antimutator" affects in regard to protein-based genetic elements. "Protein mutagens" have also been identified that affect formation and/or propagation of the alternative protein conformations. Prion-forming abilities appear to be conserved in evolution, despite the divergence of the corresponding amino acid sequences. Moreover, a wide variety of proteins ofdifferent origins appear to possess the ability to form amyloid-like aggregates, that in certain conditions might potentially result in prion-like switches. This suggests a possible mechanism for the inheritance of acquired traits, postulated in the Lamarckian theory of evolution. The prion model also puts in doubt the notion that cloned animals are genetically identical to their genome donors, and suggests that genome sequence would not providea complete information about the genetic makeup of an organism. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 07/04/20 alle ore 00:09:17