Iron Regulatory Protein 2 as Iron Sensor IRON-DEPENDENT OXIDATIVE MODIFICATION OF CYSTEINE
作者： Dae-Kyung Kang , Jinsook Jeong , Steven K. Drake , Nancy B. Wehr , Tracey A. Rouault
关键词:
摘要: Iron regulatory protein 2 coordinates cellular regulation of iron metabolism by binding to responsive elements in mRNA. The is synthesized constitutively but rapidly degraded when stores are replete. This iron-dependent degradation requires the presence a 73-residue domain, its functions have not yet been established. We now show that domain can act as an sensor, mediating own covalent modification. forms iron-binding site with three cysteine residues located middle domain. It then reacts molecular oxygen generate reactive oxidizing species at site. One residue oxidized dehydrocysteine and other products. modification may thus mark molecule for proteasome system.
sci-hub.se 参考文章(26)
K. Iwai, R. D. Klausner, T. A. Rouault, Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. The EMBO Journal. ,vol. 14, pp. 5350- 5357 ,(1995) , 10.1002/J.1460-2075.1995.TB00219.X
Tracey Rouault, Richard Klausner, Regulation of iron metabolism in eukaryotes. Current Topics in Cellular Regulation. ,vol. 35, pp. 1- 19 ,(1997) , 10.1016/S0070-2137(97)80001-5
R. Binder, J.A. Horowitz, J.P. Basilion, D.M. Koeller, R.D. Klausner, J.B. Harford, Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3' UTR and does not involve poly(A) tail shortening. The EMBO Journal. ,vol. 13, pp. 1969- 1980 ,(1994) , 10.1002/J.1460-2075.1994.TB06466.X
V.Y. Reddy, P.E. Desorchers, S.V. Pizzo, S.L. Gonias, J.A. Sahakian, R.L. Levine, S.J. Weiss, Oxidative dissociation of human alpha 2-macroglobulin tetramers into dysfunctional dimers. Journal of Biological Chemistry. ,vol. 269, pp. 4683- 4691 ,(1994) , 10.1016/S0021-9258(17)41830-8
Renji Okazaki, Chapter 5 Chemistry of thioaldehydes Organosulfur Chemistry. ,vol. 1, pp. 225- 258 ,(1995) , 10.1016/S1099-8268(07)80016-3
B. Guo, Y. Yu, E.A. Leibold, Iron regulates cytoplasmic levels of a novel iron-responsive element-binding protein without aconitase activity. Journal of Biological Chemistry. ,vol. 269, pp. 24252- 24260 ,(1994) , 10.1016/S0021-9258(19)51075-4
Rodney L Levine, Carbonyl modified proteins in cellular regulation, aging, and disease2,3 2Guest Editor: Earl Stadtman 3This article is part of a series of reviews on “Oxidatively Modified Proteins in Aging and Disease.” The full list of papers may be found on the homepage of the journal. Free Radical Biology and Medicine. ,vol. 32, pp. 790- 796 ,(2002) , 10.1016/S0891-5849(02)00765-7
Clifford Taggart, Daniel Cervantes-Laurean, Geumsoo Kim, Noel G McElvaney, Nancy Wehr, Joel Moss, Rodney L Levine, Oxidation of either Methionine 351 or Methionine 358 in α1-Antitrypsin Causes Loss of Anti-neutrophil Elastase Activity Journal of Biological Chemistry. ,vol. 275, pp. 27258- 27265 ,(2000) , 10.1074/JBC.M004850200
A.Jennifer Rivett, Rodney L. Levine, Metal-catalyzed oxidation of Escherichia coli glutamine synthetase: correlation of structural and functional changes. Archives of Biochemistry and Biophysics. ,vol. 278, pp. 26- 34 ,(1990) , 10.1016/0003-9861(90)90226-O
Shelley D. Copley, Elizabeth Frank, Wolff M. Kirsch, Tad H. Koch, Detection and possible origins of aminomalonic acid in protein hydrolysates Analytical Biochemistry. ,vol. 201, pp. 152- 157 ,(1992) , 10.1016/0003-2697(92)90188-D