Reversible protein acetylation / [editors, Gregory Bock and Jamie Goode].

Format:

Book

Conference/Event

Contributor:

Bock, Gregory.

Goode, Jamie.

Novartis Foundation.

Conference Name:

Symposium on Reversible Protein Acetylation (2003 London, England)

Series:

Novartis Foundation symposium ; 259.

Novartis Foundation symposium ; 259

Language:

English

Subjects (All):

Acetylation.

Proteins--Structure.

Proteins.

Histones.

Chromatin--Structure.

Chromatin.

Proteins--Chemical modification.

Histone deacetylase.

Protein Conformation.

Chromatin--ultrastructure.

Histone Deacetylases.

Medical Subjects:

Acetylation.

Protein Conformation.

Histones.

Chromatin--ultrastructure.

Histone Deacetylases.

Physical Description:

x, 300 pages : illustrations ; 24 cm.

Place of Publication:

Chichester ; Hoboken, NJ : Wiley, 2004.

Summary:

The reversible acetylation of lysine residues on histone proteins has emerged as a major factor in the regulation of transcription in eukaryotes. All core histone proteins are acetylated and unique functional chromosomal domains are characterized by specific patterns of acetylation within their histone proteins. Functional correlations have been established between the level of acetylation of individual genes and their transcriptional activity. These complex signals are currently being elucidated in the context of the 'histone code hypothesis'. This model posits that distinct acetylation patterns in histones, along with other post-translational modifications, serve as specific signals recognized by the nuclear transcriptional machinery. Histone acetylation is under the control of competing histone acetyltransferases (HATs) and histone deacetylases (HDACs). Both enzyme families contain many members: at least 18 distinct human HDACs have been identified. As well as regulating transcription, these proteins play critical roles in cell cycle control and differentiation. Acetylation is not restricted to histone proteins; a growing number of important biological functions appear to be regulated via acetylation. These include DNA binding (p53), nuclear-cytoplasmic shuttling (NF-[kappaB) and coactivator recruitment (HIV Tat protein). This novel research opens up new and exciting possibilities for drug design. Inhibitors have been developed that specifically target either HDACs or HATs. HDAC inhibitors exhibit selective toxicity towards tumour cells and are being developed as potential anticancer drugs. This book describes current knowledge of acetylation and features extensive discussions amongst the world's experts in this field, with an emphasis on major unanswered questions.

Contents:

Beyond the double helix: writing and reading the histone code / Yanming Wang, Wolfgang Fischle, Wang Cheung, Steven Jacobs, Sepideh Khorasanizadeh, C. David Allis 3

The indexing potential of histone lysine methylation / Gunnar Schotta, Monika Lachner, Antoine H. F. M. Peters, Thomas Jenuwein 22

A model for step-wise assembly of heterochromatin in yeast / Danesh Moazed, Adam D. Rudner, Julie Huang, Georg J. Hoppe, Jason C. Tanny 48

H2B ubiquitylation and de-ubiquitylation in gene activation / Anastasia Wyce, Karl W. Henry, Shelley L. Berger 63

Structural and chemical basis of histone acetylation / Ronen Marmorstein 78

Phosphorylation and acetylation of histone H3 at inducible genes: two controversies revisited / Louis C. Mahadevan, Alison L. Clayton, Catherine A. Hazzalin, Stuart Thomson 102

HDAC7 regulates apoptosis in developing thymocytes / Eric Verdin, Frank Dequiedt, Herb Kasler 115

Dual roles of histone deacetylases in the control of cardiac growth / Timothy A. McKinsey, Eric N. Olson 132

Chromatin modifications as clues to the regulation of antigen receptor assembly / David Ciccone, Marjorie Oettinger 146

General discussion I Histone modification in X inactivation 163

The HDAC complex and cytoskeleton / Jeffery J. Kovacs, Charlotte Hubbert, Tso-Pang Yao 170

Tat acetylation: a regulatory switch between early and late phases in HIV transcription elongation / Melanie Ott, Alexander Dorr, Claudia Hetzer-Egger, Katrin Kaehlcke, Martina Schnolzer, Peter Henklein, Phil Cole, Ming-Ming Zhou, Eric Verdin 182

Dynamics of the p53 acetylation pathway / Wei Gu, Jianyuan Luo, Chris L. Brooks, Anatoly Y. Nikolaev, Muyang Li 197

Regulation of NF-[kappa]B action by reversible acetylation / Warner C. Greene, Lin-feng Chen 208

General discussion II p300 and DNA repair 223

Reversal of gene silencing as a therapeutic target for cancer

roles for DNA methylation and its interdigitation with chromatin / Stephen B. Baylin 226

Transcription regulation by histone deacetylases / Shaowen Wang, Yan-Yan Neale, Marija Zeremski, Dalia Cohen 238

Molecular and cellular basis for the anti-proliferative effects of the HDAC inhibitor LAQ824 / Peter Atadja, Meier Hsu, Paul Kwon, Nancy Trogani, Kapil Bhalla, Stacy Remiszewski 249

Histone deacetylase inhibitors: development as cancer therapy / Paul A. Marks, Victoria M. Richon, Wm Kevin Kelly, Judy H. Chiao, Thomas Miller 269

General discussion III PML-RAR[alpha] hypermethylation in leukaemia 285.

Notes:

Proceedings of the Symposium on Reversible Protein Acetylation, held at the Novartis Foundation, London, 6-8 May, 2003.

Includes bibliographical references and indexes.

ISBN:

0470862610

OCLC:

56415160