Structural highlights
Function
[SIZ1_ORYSJ] Probable SUMO E3 ligase that may regulate Pi starvation responses (By similarity).
Publication Abstract from PubMed
We determined the three-dimensional structure of the PHD finger of the rice Siz/PIAS-type SUMO ligase, OsSiz1, by NMR spectroscopy and investigated binding ability for a variety of methylated histone H3 tails, showing that OsSiz1-PHD primarily recognizes dimethylated Arg2 of the histone H3 and that methylations at Arg2 and Lys4 reveal synergy effect on binding to OsSiz1-PHD. The K4 cage of OsSiz1-PHD for trimethylated Lys4 of H3K4me3 was similar to that of the BPTF-PHD finger, while the R2 pocket for Arg2 was different. It is intriguing that the PHD module of Siz/PIAS plays an important role, with collaboration with the DNA binding domain SAP, in gene regulation through SUMOylation of a variety of effectors associated with the methylated arginine-riched chromatin domains.
PHD finger of the SUMO ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2.,Shindo H, Suzuki R, Tsuchiya W, Taichi M, Nishiuchi Y, Yamazaki T FEBS Lett. 2012 Jun 21;586(13):1783-9. Epub 2012 May 21. PMID:22626555[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shindo H, Suzuki R, Tsuchiya W, Taichi M, Nishiuchi Y, Yamazaki T. PHD finger of the SUMO ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2. FEBS Lett. 2012 Jun 21;586(13):1783-9. Epub 2012 May 21. PMID:22626555 doi:10.1016/j.febslet.2012.04.063
