The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases.
The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases.
复制标题
DOI:
10.1038/s41589-018-0071-y
复制
发表时间:
2018-07
影响因子:
14.8
通讯作者:
Schofield CJ
中科院分区:
文献类型:
--
作者:
Markolovic S;Zhuang Q;Wilkins SE;Eaton CD;Abboud MI;Katz MJ;McNeil HE;Leśniak RK;Hall C;Struwe WB;Konietzny R;Davis S;Yang M;Ge W;Benesch JLP;Kessler BM;Ratcliffe PJ;Cockman ME;Fischer R;Wappner P;Chowdhury R;Coleman ML;Schofield CJ
Biochemical, structural, and cellular studies reveal Jumonji-C (JmjC) domain-containing 7 (JMJD7) as a 2-oxoglutarate (2OG)-dependent oxygenase catalyzing a previously unreported type of post-translational modification, (3S)-lysyl hydroxylation. Crystallographic analyses reveal JMJD7 as more closely related to the JmjC hydroxylases rather than the JmjC demethylases. Biophysical and mutation studies show that JMJD7 has a unique dimerization mode, with interactions between monomers involving both N- and C-terminal regions and disulfide bond formation. A proteomic approach identifies two related members of the Translation Factor (TRAFAC) family of GTPases, Developmentally Regulated GTP Binding Proteins 1 and 2 (DRG1/2), as activity-dependent JMJD7 interactors. Mass spectrometric analyses demonstrate that JMJD7 catalyzes Fe(II)- and 2OG-dependent hydroxylation of a highly-conserved lysine residue in DRG1/2; amino acid analyses reveal JMJD7 catalyzes (3S)-lysyl hydroxylation. The functional assignment of JMJD7 will enable future studies to define the role of DRG hydroxylation in cell growth and disease.
登录
查看更多内容
影响因子:
4.8
作者:
Elkins, JM;Hewitson, KS;Schofield, CJ
通讯作者:
Schofield, CJ
影响因子:
64.8
作者:
通讯作者:
--
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
14.9
作者:
Francis, Sandrea M.;Gas, Maria-Eugenia;Seraphin, Bertrand
通讯作者:
Seraphin, Bertrand
影响因子:
3.8
作者:
Jang SH;Kim AR;Park NH;Park JW;Han IS
通讯作者:
Han IS