Unexpected Histone H3 Tail-clipping Activity of Glutamate Dehydrogenase
作者： Papita Mandal , Naveen Verma , Sakshi Chauhan , Raghuvir S Tomar , None
关键词: Histone methyltransferase 、 Histone H3 、 Histone H2A 、 Histone deacetylase 5 、 Histone methylation 、 Histone deacetylase 2 、 Biology 、 HDAC11 、 SAP30 、 Biochemistry
摘要: Clipping of histone tails has been reported in several organisms. However, the significance and regulation tail clipping largely remains unclear. According to recent discoveries H3 found be involved gene expression chromatin dynamics. Earlier we had provided evidence tissue-specific proteolytic processing White Leghorn chicken liver nuclei. In this study identify a novel activity glutamate dehydrogenase (GDH) as H3-specific protease tissue. This is regulated by divalent ions thiol-disulfide conversion vitro. GDH specifically clips its free well chromatin-bound form. Furthermore, have an inhibitor that inhibits H3-clipping GDH. Like previously proteases, too may potential regulate/modulate post-translational modifications removing N-terminal residues histone. short, our findings unexpected specific redox state, ionic concentrations, cellular Background: Histone tissues not brain. Results: Glutamate H3. Conclusion: act modifier thereby regulates metabolism. Significance: for first time implicated epigenetic process.
sci-hub.se 参考文章(34)
Debashis Bandyopadhyay, Ajay K. Chatterjee, Asoke G. Datta, Effect of cadmium, mercury and copper on partially purified hepatic flavokinase of rat Molecular and Cellular Biochemistry. ,vol. 167, pp. 73- 80 ,(1997) , 10.1023/A:1006815504302
T H Eickbush, J E Godfrey, M C Elia, E N Moudrianakis, H2a-specific proteolysis as a unique probe in the analysis of the histone octamer. Journal of Biological Chemistry. ,vol. 263, pp. 18972- 18978 ,(1988) , 10.1016/S0021-9258(18)37377-0
T.J. Stillman, P.J. Baker, K.L. Britton, D.W. Rice, Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. Journal of Molecular Biology. ,vol. 234, pp. 1131- 1139 ,(1993) , 10.1006/JMBI.1993.1665
M C Elia, E N Moudrianakis, Regulation of H2a-specific proteolysis by the histone H3:H4 tetramer. Journal of Biological Chemistry. ,vol. 263, pp. 9958- 9964 ,(1988) , 10.1016/S0021-9258(19)81611-3
R Kaul, A Hoang, P Yau, E M Bradbury, W M Wenman, The chlamydial EUO gene encodes a histone H1-specific protease. Journal of Bacteriology. ,vol. 179, pp. 5928- 5934 ,(1997) , 10.1128/JB.179.18.5928-5934.1997
Samantha G Pattenden, Mark JK Chandy, José L Gutiérrez, Jerry L Workman, Chromatin dynamics rule the genome Genome Biology. ,vol. 6, pp. 355- 355 ,(2005) , 10.1186/GB-2005-6-11-355
J. V. Chodaparambil, R. S. Edayathumangalam, Y. Bao, Y. -J. Park, K. Luger, Nucleosome structure and function. Ernst Schering Research Foundation workshop. pp. 29- 46 ,(2006) , 10.1007/3-540-37633-X_2
M M Falk, P R Grigera, I E Bergmann, A Zibert, G Multhaup, E Beck, Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3. Journal of Virology. ,vol. 64, pp. 748- 756 ,(1990) , 10.1128/JVI.64.2.748-756.1990
Craig L Peterson, Chromatin remodeling enzymes: taming the machines. Third in review series on chromatin dynamics. EMBO Reports. ,vol. 3, pp. 319- 322 ,(2002) , 10.1093/EMBO-REPORTS/KVF075
Woo-kyoung Lee, Seungjin Shin, Soo Seock Cho, Jong-sang Park, Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum Journal of Cellular Biochemistry. ,vol. 76, pp. 244- 253 ,(2000) , 10.1002/(SICI)1097-4644(20000201)76:2<244::AID-JCB8>3.0.CO;2-K