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Volumn 281, Issue 23, 2014, Pages 5292-5308

H3 clipping activity of glutamate dehydrogenase is regulated by stefin B and chromatin structure

Author keywords

Chromatin structure; Glutamate dehydrogenase; H3 tail processing; Histone modification; Stefin B

Indexed keywords

CYSTATIN B; GLUTAMATE DEHYDROGENASE; HISTONE H3; PROTEINASE; CHROMATIN; CSTB PROTEIN, HUMAN; HISTONE;

EID: 84918840404     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.13069     Document Type: Article
Times cited : (14)

References (34)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF & Richmond TJ (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    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 84881604151 scopus 로고    scopus 로고
    • Histone variant H3.3 maintains a decondensed chromatin state essential for mouse preimplantation development
    • Lin CJ, Conti M & Ramalho-Santos M (2013) Histone variant H3.3 maintains a decondensed chromatin state essential for mouse preimplantation development. Development 140, 3624-3634.
    • (2013) Development , vol.140 , pp. 3624-3634
    • Lin, C.J.1    Conti, M.2    Ramalho-Santos, M.3
  • 4
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T (2007) Chromatin modifications and their function. Cell 128, 693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 5
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD & Allis CD (2000) The language of covalent histone modifications. Nature 403, 41-45.
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 6
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T & Allis CD (2001) Translating the histone code. Science 293, 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 7
    • 0033848849 scopus 로고    scopus 로고
    • Histone acetylation and an epigenetic code
    • Turner BM (2000) Histone acetylation and an epigenetic code. Bio Essays 22, 836-845.
    • (2000) Bio Essays , vol.22 , pp. 836-845
    • Turner, B.M.1
  • 9
    • 84879591090 scopus 로고    scopus 로고
    • Unexpected histone H3 tail-clipping activity of glutamate dehydrogenase
    • Mandal P, Verma N, Chauhan S & Tomar RS (2013) Unexpected histone H3 tail-clipping activity of glutamate dehydrogenase. J Biol Chem 288, 18743-18757.
    • (2013) J Biol Chem , vol.288 , pp. 18743-18757
    • Mandal, P.1    Verma, N.2    Chauhan, S.3    Tomar, R.S.4
  • 11
    • 84896513129 scopus 로고    scopus 로고
    • PRB1 is required for clipping of the histone H3 N-terminal tail in Saccharomyces cerevisiae
    • Xue Y, Vashisht AA, Tan Y, Su T & Wohlschlegel JA (2014) PRB1 is required for clipping of the histone H3 N-terminal tail in Saccharomyces cerevisiae. PLoS One 9, e90496.
    • (2014) PLoS One , vol.9 , pp. e90496
    • Xue, Y.1    Vashisht, A.A.2    Tan, Y.3    Su, T.4    Wohlschlegel, J.A.5
  • 12
    • 84885036973 scopus 로고    scopus 로고
    • Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro
    • Purohit JS, Tomar RS, Panigrahi AK, Pandey SM, Singh D & Chaturvedi MM (2013) Chicken liver glutamate dehydrogenase (GDH) demonstrates a histone H3 specific protease (H3ase) activity in vitro. Biochimie 95, 1999-2009.
    • (2013) Biochimie , vol.95 , pp. 1999-2009
    • Purohit, J.S.1    Tomar, R.S.2    Panigrahi, A.K.3    Pandey, S.M.4    Singh, D.5    Chaturvedi, M.M.6
  • 13
    • 0018903045 scopus 로고
    • Proteolytic processing of histone H3 in chromatin: A physiologically regulated event in Tetrahymena micronuclei
    • Allis CD, Bowen JK, Abraham GN, Glover CV & Gorovsky MA (1980) Proteolytic processing of histone H3 in chromatin: a physiologically regulated event in Tetrahymena micronuclei. Cell 20, 55-64.
    • (1980) Cell , vol.20 , pp. 55-64
    • Allis, C.D.1    Bowen, J.K.2    Abraham, G.N.3    Glover, C.V.4    Gorovsky, M.A.5
  • 14
    • 0025099730 scopus 로고
    • Foot-and-mouth disease virus protease 3C inhibits cellular transcription and mediates cleavage of histone H3
    • Tesar M & Marquardt O (1990) Foot-and-mouth disease virus protease 3C inhibits cellular transcription and mediates cleavage of histone H3. Virology 174, 364-374.
    • (1990) Virology , vol.174 , pp. 364-374
    • Tesar, M.1    Marquardt, O.2
  • 15
    • 84860460200 scopus 로고    scopus 로고
    • Identification of a novel histone H3 specific protease activity in nuclei of chicken liver
    • Mandal P, Azad GK & Tomar RS (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
  • 16
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk B, Turk V & Turk D (1997) Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol Chem 378, 141-150.
    • (1997) Biol Chem , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 18
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou EP, Pilch DR, Orr AH, Ivanova VS & Bonner WM (1998) DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 273, 5858-5868.
    • (1998) J Biol Chem , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 19
    • 84870793679 scopus 로고    scopus 로고
    • Histone H1 plays a role in heterochromatin formation and VSG expression site silencing in Trypanosoma brucei
    • Povelones ML, Gluenz E, Dembek M, Gull K & Rudenko G (2012) Histone H1 plays a role in heterochromatin formation and VSG expression site silencing in Trypanosoma brucei. PLoS Pathog 8, e1003010.
    • (2012) PLoS Pathog , vol.8 , pp. e1003010
    • Povelones, M.L.1    Gluenz, E.2    Dembek, M.3    Gull, K.4    Rudenko, G.5
  • 20
    • 14244255860 scopus 로고    scopus 로고
    • Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)
    • Swiercz R, Person MD & Bedford MT (2005) Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). Biochem J 386, 85-91.
    • (2005) Biochem J , vol.386 , pp. 85-91
    • Swiercz, R.1    Person, M.D.2    Bedford, M.T.3
  • 21
    • 3342936604 scopus 로고    scopus 로고
    • PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits
    • Bachand F & Silver PA (2004) PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. EMBO J 23, 2641-2650.
    • (2004) EMBO J , vol.23 , pp. 2641-2650
    • Bachand, F.1    Silver, P.A.2
  • 23
    • 0020597121 scopus 로고
    • Synthesis of native 60S and 40S ribosomal subunits in Yoshida rat ascites hepatoma AH-130 cells: Correlation with the rate of cell growth
    • Comolli R & Rusconi L (1983) Synthesis of native 60S and 40S ribosomal subunits in Yoshida rat ascites hepatoma AH-130 cells: correlation with the rate of cell growth. Cell Biol Int Rep 7, 161-170.
    • (1983) Cell Biol Int Rep , vol.7 , pp. 161-170
    • Comolli, R.1    Rusconi, L.2
  • 25
    • 84865280797 scopus 로고    scopus 로고
    • H3K9 and H3K14 acetylation co-occur at many gene regulatory elements, while H3K14ac marks a subset of inactive inducible promoters in mouse embryonic stem cells
    • Karmodiya K, Krebs AR, Oulad-Abdelghani M, Kimura H & Tora L (2012) H3K9 and H3K14 acetylation co-occur at many gene regulatory elements, while H3K14ac marks a subset of inactive inducible promoters in mouse embryonic stem cells. BMC Genomics 13, 424.
    • (2012) BMC Genomics , vol.13 , pp. 424
    • Karmodiya, K.1    Krebs, A.R.2    Oulad-Abdelghani, M.3    Kimura, H.4    Tora, L.5
  • 26
    • 84896933603 scopus 로고    scopus 로고
    • Histone H3 lysine 14 (H3K14) acetylation facilitates DNA repair in a positioned nucleosome by stabilizing the binding of the chromatin remodeler RSC (Remodels Structure of Chromatin
    • Duan M-R & Smerdon MJ (2014) Histone H3 lysine 14 (H3K14) acetylation facilitates DNA repair in a positioned nucleosome by stabilizing the binding of the chromatin remodeler RSC (Remodels Structure of Chromatin. J Biol Chem 289, 8353-8363.
    • (2014) J Biol Chem , vol.289 , pp. 8353-8363
    • Duan, M.-R.1    Smerdon, M.J.2
  • 27
    • 47549105301 scopus 로고    scopus 로고
    • Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair
    • Chen CC, Carson JJ, Feser J, Tamburini B, Zabaronick S, Linger J & Tyler JK (2008) Acetylated lysine 56 on histone H3 drives chromatin assembly after repair and signals for the completion of repair. Cell 134, 231-243.
    • (2008) Cell , vol.134 , pp. 231-243
    • Chen, C.C.1    Carson, J.J.2    Feser, J.3    Tamburini, B.4    Zabaronick, S.5    Linger, J.6    Tyler, J.K.7
  • 28
    • 47549092547 scopus 로고    scopus 로고
    • Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    • Li Q, Zhou H, Wurtele H, Davies B, Horazdovsky B, Verreault A & Zhang Z (2008) Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly. Cell 134, 244-255.
    • (2008) Cell , vol.134 , pp. 244-255
    • Li, Q.1    Zhou, H.2    Wurtele, H.3    Davies, B.4    Horazdovsky, B.5    Verreault, A.6    Zhang, Z.7
  • 29
    • 48249148195 scopus 로고    scopus 로고
    • Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation
    • Williams SK, Truong D & Tyler JK (2008) Acetylation in the globular core of histone H3 on lysine-56 promotes chromatin disassembly during transcriptional activation. Proc Natl Acad Sci USA 105, 9000-9005.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9000-9005
    • Williams, S.K.1    Truong, D.2    Tyler, J.K.3
  • 31
    • 33846796258 scopus 로고    scopus 로고
    • Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication
    • Han J, Zhou H, Horazdovsky B, Zhang K, Xu RM & Zhang Z (2007) Rtt109 acetylates histone H3 lysine 56 and functions in DNA replication. Science 315, 653-655.
    • (2007) Science , vol.315 , pp. 653-655
    • Han, J.1    Zhou, H.2    Horazdovsky, B.3    Zhang, K.4    Xu, R.M.5    Zhang, Z.6
  • 32
    • 0038613861 scopus 로고    scopus 로고
    • HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain
    • Meehan RR, Kao CF & Pennings S (2003) HP1 binding to native chromatin in vitro is determined by the hinge region and not by the chromodomain. EMBO J 22, 3164-3174.
    • (2003) EMBO J , vol.22 , pp. 3164-3174
    • Meehan, R.R.1    Kao, C.F.2    Pennings, S.3
  • 33
    • 0017687532 scopus 로고
    • Nuclear matrix, Isolation and characterization of a framework structure from rat liver nuclei
    • Berezney R & Coffey DS (1977) Nuclear matrix, Isolation and characterization of a framework structure from rat liver nuclei. J Cell Biol 73, 616-637.
    • (1977) J Cell Biol , vol.73 , pp. 616-637
    • Berezney, R.1    Coffey, D.S.2


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