메뉴 건너뛰기




Volumn 288, Issue 26, 2013, Pages 18743-18757

Unexpected histone H3 tail-clipping activity of glutamate dehydrogenase

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR INHIBITORS; GLUTAMATE DEHYDROGENASE; IONIC CONCENTRATIONS; POST-TRANSLATIONAL MODIFICATIONS; PROTEASE ACTIVITIES; PROTEOLYTIC ACTIVITIES; PROTEOLYTIC PROCESSING; TISSUE SPECIFICS;

EID: 84879591090     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.462531     Document Type: Article
Times cited : (35)

References (34)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., and Richmond, T. J. (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389, 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mäder, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 1942502793 scopus 로고    scopus 로고
    • Role of Histone Tails in the Conformation and Interactions of Nucleosome Core Particles
    • DOI 10.1021/bi036210g
    • Bertin, A., Leforestier, A., Durand, D., and Livolant, F. (2004) Role of histone tails in the conformation and interactions of nucleosome core particles. Biochemistry 43, 4773-4780 (Pubitemid 38509098)
    • (2004) Biochemistry , vol.43 , Issue.16 , pp. 4773-4780
    • Bertin, A.1    Leforestier, A.2    Durand, D.3    Livolant, F.4
  • 3
    • 67650725820 scopus 로고    scopus 로고
    • The biology of chromatin remodeling complexes
    • Clapier, C. R., and Cairns, B. R. (2009) The biology of chromatin remodeling complexes. Annu. Rev. Biochem. 78, 273-304
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 273-304
    • Clapier, C.R.1    Cairns, B.R.2
  • 6
    • 0033994292 scopus 로고    scopus 로고
    • ATP-dependent chromatin-remodeling complexes
    • DOI 10.1128/MCB.20.6.1899-1910.2000
    • Vignali, M., Hassan, A. H., Neely, K. E., and Workman, J. L. (2000) ATP-dependent chromatin-remodeling complexes. Nat. Rev. Mol. Cell. Biol. 20, 1899-1910 (Pubitemid 30123807)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.6 , pp. 1899-1910
    • Vignali, M.1    Hassan, A.H.2    Neely, K.E.3    Workman, J.L.4
  • 7
    • 61549091854 scopus 로고    scopus 로고
    • Nucleosome shape dictates chromatin fiber structure
    • Depken, M., and Schiessel, H. (2009) Nucleosome shape dictates chromatin fiber structure. Biophys. J. 96, 777-784
    • (2009) Biophys. J. , vol.96 , pp. 777-784
    • Depken, M.1    Schiessel, H.2
  • 8
    • 0035937419 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes stabilize SWI/SNF binding to promoter nucleosomes
    • DOI 10.1016/S0092-8674(01)00279-3
    • Hassan, A. H., Neely, K. E., and Workman, J. L. (2001) Histone acetyltransferase complexes stabilize swi/snf binding to promoter nucleosomes. Cell 104, 817-827 (Pubitemid 32289275)
    • (2001) Cell , vol.104 , Issue.6 , pp. 817-827
    • Hassan, A.H.1    Neely, K.E.2    Workman, J.L.3
  • 9
    • 33947532026 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes: One size doesn't fit all
    • DOI 10.1038/nrm2145, PII NRM2145
    • Lee, K. K., and Workman, J. L. (2007) Histone acetyltransferase complexes. One size doesn't fit all. Nat. Rev. Mol. Cell. Biol. 8, 284-295 (Pubitemid 46474661)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.4 , pp. 284-295
    • Lee, K.K.1    Workman, J.L.2
  • 11
    • 0036256125 scopus 로고    scopus 로고
    • Chromatin remodeling enzymes. Taming the machines. Third in review series on chromatin dynamics
    • Peterson, C. L. (2002) Chromatin remodeling enzymes. Taming the machines. Third in review series on chromatin dynamics. EMBO Rep. 3, 319-322
    • (2002) EMBO Rep. , vol.3 , pp. 319-322
    • Peterson, C.L.1
  • 12
    • 0017291792 scopus 로고
    • A chromatin-bound proteolytic activity with unique specificity for histone H2A
    • Eickbush, T. H., Watson, D. K., and Moudrianakis, E. N. (1976) A chromatin-bound proteolytic activity with unique specificity for histone H2A. Cell 9, 785-792
    • (1976) Cell , vol.9 , pp. 785-792
    • Eickbush, T.H.1    Watson, D.K.2    Moudrianakis, E.N.3
  • 13
    • 0023690281 scopus 로고
    • Regulation of H2a-specific proteolysis by the histone H3:H4 tetramer
    • Elia, M. C., and Moudrianakis, E. N. (1988) Regulation of H2a-specific proteolysis by the histone H3:H4 tetramer. J. Biol. Chem. 263, 9958-9964
    • (1988) J. Biol. Chem. , vol.263 , pp. 9958-9964
    • Elia, M.C.1    Moudrianakis, E.N.2
  • 14
    • 0024268331 scopus 로고
    • H2a-specific proteolysis as a unique probe in the analysis of the histone octamer
    • Eickbush, T. H., Godfrey, J. E., Elia, M. C., and Moudrianakis, E. N. (1988) H2a-specific proteolysis as a unique probe in the analysis of the histone octamer. J. Biol. Chem. 263, 18972-18978 (Pubitemid 19016358)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.35 , pp. 18972-18978
    • Eickbush, T.H.1    Godfrey, J.E.2    Elia, M.C.3    Moudrianakis, E.N.4
  • 15
    • 0030883567 scopus 로고    scopus 로고
    • The Chlamydial EUO gene encodes a histone H1-specific protease
    • Kaul, R., Hoang, A., Yau, P., Bradbury, E. M., and Wenman, W. M. (1997) The chlamydial EUO gene encodes a histone H1-specific protease. J. Bacteriol. 179, 5928-5934 (Pubitemid 27398297)
    • (1997) Journal of Bacteriology , vol.179 , Issue.18 , pp. 5928-5934
    • Kaul, R.1    Hoang, A.2    Yau, P.3    Bradbury, E.M.4    Wenman, W.M.5
  • 16
    • 0018903045 scopus 로고
    • Proteolytic processing of histone H3 in chromatin: A physiologically regulated event in Tetrahymena micronuclei
    • Allis, C. D., Bowen, J. K., Abraham, G. N., Glover, C. V., and Gorovsky, M. A. (1980) Proteolytic processing of histone H3 in chromatin. A physiologically regulated event in Tetrahymena micronuclei. Cell 20, 55-64 (Pubitemid 10117300)
    • (1980) Cell , vol.20 , Issue.1 , pp. 55-64
    • Allis, C.D.1    Abraham, G.N.2    Bowen, J.K.3
  • 17
    • 0021279495 scopus 로고
    • Proteolytic processing of micronuclear H3 and histone phosphorylation during conjugation in Tetrahymena thermophila
    • Allis, C. D., and Wiggins, J. C. (1984) Proteolytic processing of micronuclear H3 and histone phosphorylation during conjugation in Tetrahymena thermophila. Exp. Cell Res. 153, 287-298 (Pubitemid 14089823)
    • (1984) Experimental Cell Research , vol.153 , Issue.2 , pp. 287-298
    • Allis, C.D.1    Wiggins, J.C.2
  • 18
    • 0021738922 scopus 로고
    • Proteolytic processing of H1-like histones in chromatin: A physiologically and developmentally regulated event in Tetrahymena micronuclei
    • DOI 10.1083/jcb.99.5.1669
    • Allis, C. D., Allen, R. L., Wiggins, J. C., Chicoine, L. G., and Richman, R. (1984) Proteolytic processing of h1-like histones in chromatin. A physiologically and developmentally regulated event in Tetrahymena micronuclei. J. Cell Biol. 99, 1669-1677 (Pubitemid 15223603)
    • (1984) Journal of Cell Biology , vol.99 , Issue.5 , pp. 1669-1677
    • Allis, C.D.1    Allen, R.L.2    Wiggins, J.C.3
  • 20
    • 0025190848 scopus 로고
    • Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3
    • Falk, M. M., Grigera, P. R., Bergmann, I. E., Zibert, A., Multhaup, G., and Beck, E. (1990) Foot-and-mouth disease virus protease 3C induces specific proteolytic cleavage of host cell histone H3. J. Virol. 64, 748-756 (Pubitemid 20032691)
    • (1990) Journal of Virology , vol.64 , Issue.2 , pp. 748-756
    • Falk, M.M.1    Grigera, P.R.2    Bergmann, I.E.3    Zibert, A.4    Multhaup, G.5    Beck, E.6
  • 21
    • 0025099730 scopus 로고
    • Foot-and-mouth disease virus protease 3C inhibits cellular transcription and mediates cleavage of histone H3
    • DOI 10.1016/0042-6822(90)90090-E
    • Tesar, M., and Marquardt, O. (1990) Foot-and-mouth disease virus protease 3C inhibits cellular transcription and mediates cleavage of histone H3. Virology 174, 364-374 (Pubitemid 20060140)
    • (1990) Virology , vol.174 , Issue.2 , pp. 364-374
    • Tesar, M.1    Marquardt, O.2
  • 22
    • 0033988512 scopus 로고    scopus 로고
    • Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham, G. J., McInerney, G. M., and Ross-Smith, N. (2000) Foot-andmouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J. Virol. 74, 272-280 (Pubitemid 30002907)
    • (2000) Journal of Virology , vol.74 , Issue.1 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 23
  • 25
    • 84860460200 scopus 로고    scopus 로고
    • Identification of a novel histone H3 specific protease activity in nuclei of chicken liver
    • Mandal, P., Azad, G. K., and Tomar, R. S. (2012) Identification of a novel histone H3 specific protease activity in nuclei of chicken liver. Biochem. Biophys. Res. Commun. 421, 261-267
    • (2012) Biochem. Biophys. Res. Commun. , vol.421 , pp. 261-267
    • Mandal, P.1    Azad, G.K.2    Tomar, R.S.3
  • 26
    • 0033427740 scopus 로고    scopus 로고
    • Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum
    • DOI 10.1002/(SICI)1097-4644(20000201)76:2<244::AID
    • Lee, W. K., Shin, S., Cho, S. S., and Park, J. S. (1999) Purification and characterization of glutamate dehydrogenase as another isoprotein binding to the membrane of rough endoplasmic reticulum. J. Cell. Biochem. 76, 244-253 (Pubitemid 30030772)
    • (1999) Journal of Cellular Biochemistry , vol.76 , Issue.2 , pp. 244-253
    • Lee, W.-K.1    Shin, S.2    Cho, S.S.3    Park, J.-S.4
  • 27
    • 0036301509 scopus 로고    scopus 로고
    • The DNA-binding activity of protein disulfide isomerase ERp57 is associated with the a′ domain
    • DOI 10.1016/S0006-291X(02)00634-4, PII S0006291X02006344
    • Grillo, C., Coppari, S., Turano, C., and Altieri, F. (2002) The DNA-binding activity of protein disulfide isomerase ERp57 is associated with the a(′) domain. Biochem. Biophys. Res. Commun. 295, 67-73 (Pubitemid 34743776)
    • (2002) Biochemical and Biophysical Research Communications , vol.295 , Issue.1 , pp. 67-73
    • Grillo, C.1    Coppari, S.2    Turano, C.3    Altieri, F.4
  • 28
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 29
    • 33750710126 scopus 로고    scopus 로고
    • Identifying novel proteins recognizing histone modifications using peptide pull-down assay
    • Wysocka, J. (2006) Identifying novel proteins recognizing histone modifications using peptide pull-down assay. Methods 40, 339-343
    • (2006) Methods , vol.40 , pp. 339-343
    • Wysocka, J.1
  • 30
    • 0037449705 scopus 로고    scopus 로고
    • Direct association of p300 with unmodified H3 and H4 N termini modulates p300-dependent acetylation and transcription of nucleosomal templates
    • DOI 10.1074/jbc.M209355200
    • An, W., and Roeder, R. G. (2003) Direct association of p300 with unmodified H3 and H4 N termini modulates p300-dependent acetylation and transcription of nucleosomal templates. J. Biol. Chem. 278, 1504-1510 (Pubitemid 36801377)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.3 , pp. 1504-1510
    • An, W.1    Roeder, R.G.2
  • 31
    • 0031058982 scopus 로고    scopus 로고
    • Effect of cadmium, mercury and copper on partially purified hepatic flavokinase of rat
    • DOI 10.1023/A:1006815504302
    • Bandyopadhyay, D., Chatterjee, A. K., and Datta, A. G. (1997) Effect of cadmium, mercury and copper on partially purified hepatic flavokinase of rat. Mol. Cell. Biochem. 167, 73-80 (Pubitemid 27081334)
    • (1997) Molecular and Cellular Biochemistry , vol.167 , Issue.1-2 , pp. 73-80
    • Bandyopadhyay, D.1    Chatterjee, A.K.2    Datta, A.G.3
  • 33
    • 0027769953 scopus 로고
    • Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis
    • Stillman, T. J., Baker, P. J., Britton, K. L., and Rice, D. W. (1993) Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. J. Mol. Biol. 234, 1131-1139
    • (1993) J. Mol. Biol. , vol.234 , pp. 1131-1139
    • Stillman, T.J.1    Baker, P.J.2    Britton, K.L.3    Rice, D.W.4
  • 34
    • 0036549657 scopus 로고    scopus 로고
    • Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis. Cloning and comparison with two marine hyperthermophilic GDHs
    • Lee, M. K., González, J. M., and Robb, F. T. (2002) Extremely thermostable glutamate dehydrogenase (GDH) from the freshwater archaeon Thermococcus waiotapuensis. Cloning and comparison with two marine hyperthermophilic GDHs. Extremophiles 6, 151-159
    • (2002) Extremophiles , vol.6 , pp. 151-159
    • Lee, M.K.1    González, J.M.2    Robb, F.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.