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- W3090236114 abstract "Histone lysine demethylases (KDMs) play a vital role in regulating chromatin dynamics and transcription. KDM proteins are given modular activities by its sequence motifs with obvious roles division, which endow the complex and diverse functions. In our review, according to functional features, we classify sequence motifs into four classes: catalytic motifs, targeting motifs, regulatory motifs and potential motifs. JmjC, as the main catalytic motif, combines to Fe2+ and α-ketoglutarate by residues H-D/E-H and S-N-N/Y-K-N/Y-T/S. Targeting motifs make catalytic motifs recognize specific methylated lysines, such as PHD that helps KDM5 to demethylate H3K4me3. Regulatory motifs consist of a functional network. For example, NLS, Ser-rich, TPR and JmjN motifs regulate the nuclear localization. And interactions through the CW-type-C4H2C2-SWIRM are necessary to the demethylase activity of KDM1B. Additionally, many conservative domains that have potential functions but no deep exploration are reviewed for the first time. These conservative domains are usually amino acid-rich regions, which have great research value. The arrangements of four types of sequence motifs generate that KDM proteins diversify toward modular activities and biological functions. Finally, we draw a blueprint of functional mechanisms to discuss the modular activity of KDMs." @default.
- W3090236114 created "2020-10-08" @default.
- W3090236114 creator A5000742700 @default.
- W3090236114 creator A5008125789 @default.
- W3090236114 creator A5041380713 @default.
- W3090236114 creator A5079706371 @default.
- W3090236114 creator A5085618650 @default.
- W3090236114 date "2020-09-29" @default.
- W3090236114 modified "2023-10-16" @default.
- W3090236114 title "Modular arrangements of sequence motifs determine the functional diversity of KDM proteins" @default.
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