Data di Pubblicazione:
2010
Citazione:
Ni(II)-Histone H4 Interactions : Structural Modifications / Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella. - (2010), pp. OC16.52-OC16.52. (Intervento presentato al convegno ISMEC2010 International Symposium on Metal Complexes XXI Italian-Spanish Congress on Thermodynamics of Metal Complexes tenutosi a Bilbao nel 7-11 giugno 2010).
Abstract:
It is known that nickel participates to carcinogenic processes through mechanisms interfering
with several cellular targets; among them, histone H4 has been recently identified. Histones are
nuclear proteins that package and organize DNA into nucleosomes and chromatin, but they are
also involved in gene regulation and transcription. By undergoing post-translational
modifications, such as acetylation, methylation and phosphorylation, they change chromatin
structure helping gene transcription or inhibition. Nickel showed to be in vivo a potent inhibitor of
histone H4 acetylation. Acetylation causes important structural modifications in histones : for
instance, it increases the α-helix content, thus decreasing the length of the histone tail and
affecting the transcription mechanisms.
Following these indications, we studied how nickel interacts with the histone H4 tail, investigating
the coordination mode of this metal to the the N-terminus of H4 where the sites of acetylation are
clustered. [L. Broday et al., 2000], [M.A. Zoroddu et al., 2000, 2002, 2007]
Lately we have expanded the scope of our research to the structural modifications involving the
whole protein. [M.A. Zoroddu et al., 2010]
From the study carried out by the use of several spectroscopic techniques (multidimensional
NMR, CD) we found that nickel is able to induce a secondary structure in the protein; in
particular, nickel induces an increase in α-helical conformation of the non-acetylated histone H4.
with several cellular targets; among them, histone H4 has been recently identified. Histones are
nuclear proteins that package and organize DNA into nucleosomes and chromatin, but they are
also involved in gene regulation and transcription. By undergoing post-translational
modifications, such as acetylation, methylation and phosphorylation, they change chromatin
structure helping gene transcription or inhibition. Nickel showed to be in vivo a potent inhibitor of
histone H4 acetylation. Acetylation causes important structural modifications in histones : for
instance, it increases the α-helix content, thus decreasing the length of the histone tail and
affecting the transcription mechanisms.
Following these indications, we studied how nickel interacts with the histone H4 tail, investigating
the coordination mode of this metal to the the N-terminus of H4 where the sites of acetylation are
clustered. [L. Broday et al., 2000], [M.A. Zoroddu et al., 2000, 2002, 2007]
Lately we have expanded the scope of our research to the structural modifications involving the
whole protein. [M.A. Zoroddu et al., 2010]
From the study carried out by the use of several spectroscopic techniques (multidimensional
NMR, CD) we found that nickel is able to induce a secondary structure in the protein; in
particular, nickel induces an increase in α-helical conformation of the non-acetylated histone H4.
Tipologia CRIS:
4.2 Abstract in Atti di convegno
Keywords:
Histone H4, nickel interactions
Elenco autori:
Zoroddu, Maria Antonietta; Peana, Massimiliano Francesco; Medici, Serenella
Link alla scheda completa:
Titolo del libro:
ISMEC2010 International Symposium on Metal Complexes XXI Italian-Spanish Congress on Thermodynamics of Metal Complexes, Book of abstracts