Reference "Comparative analysis of SET domain proteins in maize and Arabidopsis reveals multiple duplications preceding the divergence of monocots and dicots"

Reference ID

8446

Title

Comparative analysis of SET domain proteins in maize and Arabidopsis reveals multiple duplications preceding the divergence of monocots and dicots

Source

Plant physiology, 2003, vol. 132, pp. 907-925

Authors (8)

Springer-N-M	Napoli-C-A
Selinger-D-A	Pandey-R
Cone-K-C	Chandler-V-L
Kaeppler-H-F	Kaeppler-S-M

Abstract

Histone proteins play a central role in chromatin packaging, and modification of
histones is associated with chromatin accessibility. SET domain [Su(var)3-9, Enhancer-of-
zeste, Trithorax] proteins are one class of proteins that have been implicated
in regulating gene expression through histone methylation. The relationships of
22 SET domain proteins from maize (Zea mays) and 32 SET domain proteins from
Arabidopsis were evaluated by phylogenetic analysis and domain organization. Our
analysis reveals five classes of SET domain proteins in plants that can be
further divided into 19 orthology groups. In some cases, such as the Enhancer of
zeste-like and trithorax-like proteins, plants and animals contain homologous
proteins with a similar organization of domains outside of the SET domain.
However, a majority of plant SET domain proteins do not have an animal homolog
with similar domain organization, suggesting that plants have unique mechanisms
to establish and maintain chromatin states. Although the domains present in
plant and animal SET domain proteins often differ, the domains found in the
plant proteins have been generally implicated in protein-protein interactions,
indicating that most SET domain proteins operate in complexes. Combined analysis
of the maize and Arabidopsis SET domain proteins reveals that duplication of SET
domain proteins in plants is extensive and has occurred via multiple mechanisms
that preceded the divergence of monocots and dicots.