Unsafe SETs: histone lysine methyltransferases and cancer
R Schneider, AJ Bannister, T Kouzarides - Trends in biochemical sciences, 2002 - cell.com
R Schneider, AJ Bannister, T Kouzarides
Trends in biochemical sciences, 2002•cell.comEnzymes that covalently modify histones control many cellular processes by affecting gene
expression. A new class of these enzymes is the histone lysine methyltransferase family,
whose catalytic activity lies within a conserved domain, the SET domain. This article surveys
the evidence for a connection between SET-domain-containing proteins and cancer. It
proposes that deregulation of SET-domain function has an important role in carcinogenesis.
expression. A new class of these enzymes is the histone lysine methyltransferase family,
whose catalytic activity lies within a conserved domain, the SET domain. This article surveys
the evidence for a connection between SET-domain-containing proteins and cancer. It
proposes that deregulation of SET-domain function has an important role in carcinogenesis.
Abstract
Enzymes that covalently modify histones control many cellular processes by affecting gene expression. A new class of these enzymes is the histone lysine methyltransferase family, whose catalytic activity lies within a conserved domain, the SET domain. This article surveys the evidence for a connection between SET-domain-containing proteins and cancer. It proposes that deregulation of SET-domain function has an important role in carcinogenesis.
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