Data di Pubblicazione:
2005
Citazione:
Structure and Recognition in the BARS/CtBP-dependent Transcription Regulation / M. Bolognesi, M. Nardini. - In: ACTA CRYSTALLOGRAPHICA. SECTION A, FOUNDATIONS OF CRYSTALLOGRAPHY. - ISSN 0108-7673. - A61:C1(2005). ((Intervento presentato al 20. convegno 20. Congress of the International Union of Crystallography tenutosi a Firenze nel 2005.
Abstract:
BARS/CtBP3 is a dual function protein acting as acyl-transferase
in the Golgi apparatus (supporting membrane reshaping and vesicle
traffic), and as transcription co-repressor, in the nucleus, through
the interaction with several enzymatic partners (e.g. histone
deacetylases, HDACs). BARS/CtBP3 is based on a 3-domain
structure, hosting a classical dehydrogenase fold. Regulation of the
two activities is achieved through competitive binding of
NAD(H)/acyl-CoA, association equilibria, SUMO-ylation, and
eventually through recognition of specific sequence motifs in the
interacting partners. Binding of specific transcription factors to each
subunit in the dimeric BARS/CtBP3, through a PXDLS sequence
motif, is considered one of the basic mechanisms to recruit HDACs,
and modify the chromatin structure, with ensuing transcription
repression. Structural considerations and mutant analyses indicate
that different recognition sites are present on BARS/CtBP3 surface, in
keeping with its pivotal role within a nuclear protein complex hosting
more than twenty different proteins.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
biomolecular recognition, enzyme function,
transcription regulation
Elenco autori:
M. Bolognesi, M. Nardini
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