Many keys to push: diversifying the 'readership' of plant homeodomain fingers.

Yuanyuan Li, Haitao Li

Journal: Acta biochimica et biophysica Sinica 2012;44(1):28-39

PMID: 22194011

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Abstract

Covalent histone modifications-referred to as the 'histone code', are recognized by a wealth of effector or 'reader' modules, representing one of the most fundamental epigenetic regulatory mechanisms that govern the structure and function of our genome. Recent progresses on combinatorial readout of such 'histone code' promote us to reconsider epigenetic regulation as a more complicated theme than we originally anticipated. In particular, plant homeodomain (PHD) fingers, which are evolved with fine-tuned residue composition and integrated or paired with other reader modules, display remarkably diverse 'readership' other than its founding-member target, histone H3 trimethylation on lysine 4 (H3K4me3). In this review, we detail the latest progresses of PHD finger research, especially from the perspective of structural biology, and highlight the versatile binding features and biological significance of PHD fingers.

Address: Center for Structural Biology, School of Life Sciences and School of Medicine, Tsinghua University, Beijing, China.

DOI: 10.1093/abbs/gmr117

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MeSH Terms: Amino Acid Motifs, Amino Acid Sequence, DNA-Binding Proteins, Epigenesis, Genetic, Histone Code, Histones, Homeodomain Proteins, Humans, Lysine, Methylation, Models, Molecular, Plant Proteins, Plants, Protein Processing, Post-Translational, SUMO-1 Protein, Sequence Alignment, Ubiquitin-Protein Ligases