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A novel zinc-binding motif revealed by solution structures of DNA-binding domains of Arabidopsis SBP-family transcription factors 总被引:3,自引:0,他引:3
Yamasaki K Kigawa T Inoue M Tateno M Yamasaki T Yabuki T Aoki M Seki E Matsuda T Nunokawa E Ishizuka Y Terada T Shirouzu M Osanai T Tanaka A Seki M Shinozaki K Yokoyama S 《Journal of molecular biology》2004,337(1):49-63
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DNA binding and gene activation properties of the Nmp4 nuclear matrix transcription factors 总被引:5,自引:0,他引:5
Torrungruang K Alvarez M Shah R Onyia JE Rhodes SJ Bidwell JP 《The Journal of biological chemistry》2002,277(18):16153-16159
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OSCAR: one-class SVM for accurate recognition of cis-elements 总被引:1,自引:0,他引:1
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Dalle-Donne I Carini M Vistoli G Gamberoni L Giustarini D Colombo R Maffei Facino R Rossi R Milzani A Aldini G 《Free radical biology & medicine》2007,42(5):583-598
We have recently shown that actin can be modified by the Michael addition of 4-hydroxynonenal to Cys374. Here, we have exposed purified actin at increasing acrolein concentrations and have identified the sites of acrolein addition using LC-ESI-MS/MS. Acrolein reacted with Cys374, His87, His173, and, minimally, His40. Cys374 adduction by both 4-hydroxynonenal and acrolein negligibly affected the polymerization of aldehyde-modified (carbonylated) actin, as shown by fluorescence measurements. Differently, acrolein binding at histidine residues, when Cys374 was completely saturated, inhibited polymerization in a dose-dependent manner. Molecular modeling analyses indicated that structural distortions of the ATP-binding site, induced by four acrolein-Michael adducts, could explain the changes in the polymerization process. Aldehyde binding to Cys374 does not alter significantly actin polymerization because this residue is located in a very flexible region, whose covalent modifications do not alter the protein folding. These data demonstrate that Cys374 represents the primary target site of alpha,beta-unsaturated aldehyde addition to actin in vitro. As Cys374 is a preferential target for various oxidative/nitrosative modifications, and actin is one of the main carbonylated proteins in vivo, these findings also suggest that the highly reactive Cys374 could serve as a carbonyl scavenger of reactive alpha,beta-unsaturated aldehydes and other electrophilic lipids. 相似文献