INVESTIGADORES
BINOLFI Andres
artículos
Título:
Bacterial in-cell NMR of human alpha-synuclein: a disordered monomer by nature?
Autor/es:
ANDRÉS BINOLFI; FRANCOIS-XAVIER THEILLET; PHILIPP SELENKO
Revista:
BIOCHEMICAL SOCIETY TRANSACTIONS
Editorial:
PORTLAND PRESS LTD
Referencias:
Lugar: Londres; Año: 2012 vol. 40 p. 950 - 954
ISSN:
0300-5127
Resumen:
The notion
that human alpha-synuclein is an intrinsically disordered monomeric protein was
recently challenged by a postulated alpha-helical tetramer as the
physiologically relevant protein structure. The fact that this alleged
conformation had evaded detection for so many years was primarily attributed to
a widely used denaturation protocol to purify recombinant alpha-synuclein. In
the present paper, we provide in-cell NMR evidence obtained directly in intact
Escherichia coli cells that challenges a tetrameric conformation under native
in vivo conditions. Although our data cannot rule out the existence of other
intracellular protein states, especially in cells of higher organisms, they
indicate clearly that inside E. coli alpha-synuclein is mostly monomeric and
disordered.