Med Sci (Paris)
Volume 21, Number 6-7, Juin–Juillet 2005
|Page(s)||563 - 568|
|Published online||15 June 2005|
Le repliement des protéines : seconde traduction du message génétique
Protein folding: the second translation of the genetic message
Unité de repliement et modélisation des protéines, Institut Pasteur, 28, rue du Docteur Roux, 75724 Paris Cedex 15, France
Translation of the message encoded in a gene proceeds in two steps: one translates the gene’s base sequence into the protein’s aminoacid sequence; the second translates the latter into a complex, very precisely defined folded structure, the single one endowed with the specific biological properties. The second step, named « protein folding », is currently a central issue in biological research. The present editorial introduces a series of articles dedicated to this problem. It gives a brief historical overview of how our understanding of the folding mechanisms has evolved, which will be described in more details by J. Yon-Kahn. It also places the problem of protein folding in the context of basic research and its applications in several domains: (1) medicine, where folding diseases (reviewed by G. Grateau) and in particular neurodegenerative diseases caused by prions (see article by R. Melki), are more and more recognized as a public health issue ; (2) biotechnology, where the production of recombinant proteins for research, diagnostic or therapy purposes is often hampered by misfolding when a protein is expressed at high concentration in a foreign host (modern approaches to overcome this difficulty will be discussed by J.M. Betton and A. Chaffotte, and the way in which « chaperones » prevent misfolding in the cell under natural conditions will be described by A.P. Arrigo) ; (3) postgenomics, where the interpretation of the immense amount of base-sequence information collected through genome sequencing needs to be translated as rapidly as possible into structural and functional information (the computer approaches used to predict the 3D structure of a protein from its aminoacid sequence will be outlined by T. Simonson). This series comes timely, at a moment when the efforts of experimentalists, theoriticians, and « users » of protein folding start converging, and boost the power of molecular biology.
© 2005 médecine/sciences - Inserm / SRMS
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