It has been widely debated whether class IIa HDACs have catalytic deacetylase activity, and whether this plays any part in controlling gene expression. Herein, it has been demonstrated that class IIa HDACs isolated from mammalian cells are contaminated with other deacetylases, but can be prepared cleanly in Escherichia coli. These bacteria preparations have weak but measurable deacetylase activity. The low efficiency can be restored either by: mutation of an active site histidine to tyrosine, or by the use of a non-acetylated lysine substrate, allowing the development of assays to identify class IIa HDAC inhibitors.

Probing the elusive catalytic activity of vertebrate class IIa histone deacetylases / P. Jones, S. Altamura, R. De Francesco, P. Gallinari, A. Lahm, P. Neddermann, M. Rowley, S. Serafini, C. Steinkühler. - In: BIOORGANIC & MEDICINAL CHEMISTRY LETTERS. - ISSN 0960-894X. - 18:6(2008), pp. 1814-1819. [10.1016/j.bmcl.2008.02.025]

Probing the elusive catalytic activity of vertebrate class IIa histone deacetylases

R. De Francesco;
2008

Abstract

It has been widely debated whether class IIa HDACs have catalytic deacetylase activity, and whether this plays any part in controlling gene expression. Herein, it has been demonstrated that class IIa HDACs isolated from mammalian cells are contaminated with other deacetylases, but can be prepared cleanly in Escherichia coli. These bacteria preparations have weak but measurable deacetylase activity. The low efficiency can be restored either by: mutation of an active site histidine to tyrosine, or by the use of a non-acetylated lysine substrate, allowing the development of assays to identify class IIa HDAC inhibitors.
inhibitors; hypertrophy; regulators; family; HDAC7
Settore BIO/11 - Biologia Molecolare
2008
Article (author)
File in questo prodotto:
File Dimensione Formato  
Jones et al 2008.pdf

accesso riservato

Tipologia: Publisher's version/PDF
Dimensione 180.67 kB
Formato Adobe PDF
180.67 kB Adobe PDF   Visualizza/Apri   Richiedi una copia
Pubblicazioni consigliate

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/662290
Citazioni
  • ???jsp.display-item.citation.pmc??? 35
  • Scopus 86
  • ???jsp.display-item.citation.isi??? 85
social impact