Recommend Cell Cycle to your librarian for 2008. Download form here.

Sign up for Table of Contents Alerts.

home subscribe search archive forthcoming

Email this page Print this page

Review

The Diverse Biological Roles of MYST Histone Acetyltransferase Family Proteins

Tim Thomas and Anne K. Voss

volume 6 | issue 6

15 March 2007
Pages: 696 - 704

We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.

Regulation of gene expression is intimately connected to post-translational modification of histones bound to DNA. One important type of modification is acetylation of lysine residues of the N-terminal "tails". Because of the central role that covalent modifications like acetylation play in gene regulation, it is no wonder that there has been considerable interest directed towards identifying and characterizing the enzymes that catalyze these modifications. The MYST family is the largest but, until recently, one of the least well studied families of histone acetyltransferases. Experiments performed in the last few years show that MYST family proteins have a fascinating and diverse range of functions affecting almost all cellular phenomena. MYST family proteins have central and specific roles in regulating diverse cellular processes ranging from apoptosis, cell cycle and adult stem cell homeostasis to patterning of the early embryo. Since these are fundamental cellular processes it is not surprising that mutations in MYST genes are also associated with pathological conditions such as leukemia.

Authors

Tim Thomas

The Walter and Eliza Hall Institute of Medical Research; Parkville, Victoria, Australia

Anne K. Voss

The Walter and Eliza Hall Institute of Medical Research; Parkville, Victoria, Australia



We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
 Download PDF

If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.