메뉴 건너뛰기




Volumn 361, Issue 1, 2007, Pages 55-61

Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24

Author keywords

Histone deacetylase; Protein expression; Tca HDAC; Thermus caldophilus; Trichostatin A

Indexed keywords

GLUTATHIONE TRANSFERASE; HISTONE DEACETYLASE 1; HISTONE DEACETYLASE INHIBITOR; TRICHOSTATIN A; ZINC ION;

EID: 34547114742     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.147     Document Type: Article
Times cited : (5)

References (27)
  • 2
    • 0035662888 scopus 로고    scopus 로고
    • Structure of histone deacetylases: insights into substrate recognition and catalysis
    • Marmorstein R. Structure of histone deacetylases: insights into substrate recognition and catalysis. Structure 9 (2001) 1127-1133
    • (2001) Structure , vol.9 , pp. 1127-1133
    • Marmorstein, R.1
  • 3
    • 0030812917 scopus 로고    scopus 로고
    • Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily
    • Leipe D.D., and Landsman D. Histone deacetylases, acetoin utilization proteins and acetylpolyamine amidohydrolases are members of an ancient protein superfamily. Nucl. Acids Res. 25 (1997) 3693-3697
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3693-3697
    • Leipe, D.D.1    Landsman, D.2
  • 4
    • 0031434997 scopus 로고    scopus 로고
    • The origin and utility of histone deacetylase
    • Khochbin S., and Wolffe A.P. The origin and utility of histone deacetylase. FEBS Lett. 419 (1997) 157-160
    • (1997) FEBS Lett. , vol.419 , pp. 157-160
    • Khochbin, S.1    Wolffe, A.P.2
  • 5
    • 0032940072 scopus 로고    scopus 로고
    • Histone deacetylase: transcriptional repression with SINers and NuRDs
    • Ayer D.E. Histone deacetylase: transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9 (1999) 193-198
    • (1999) Trends Cell Biol. , vol.9 , pp. 193-198
    • Ayer, D.E.1
  • 6
    • 0034045040 scopus 로고    scopus 로고
    • Histone deacetylases, transcriptional control, and cancer
    • Cress W.D., and Seto E. Histone deacetylases, transcriptional control, and cancer. J. Cell Physiol. 184 (2000) 1-16
    • (2000) J. Cell Physiol. , vol.184 , pp. 1-16
    • Cress, W.D.1    Seto, E.2
  • 8
    • 0033180082 scopus 로고    scopus 로고
    • Analysis of the NuRD subunits reveals an histone deacetylase core complex and a connection with DNA methylation
    • Zhang Y., Ng H.H., Erdjument-Bromage H., Tempst P., Bird A., and Reinberg D. Analysis of the NuRD subunits reveals an histone deacetylase core complex and a connection with DNA methylation. Genes Dev. 13 (1999) 1924-1935
    • (1999) Genes Dev. , vol.13 , pp. 1924-1935
    • Zhang, Y.1    Ng, H.H.2    Erdjument-Bromage, H.3    Tempst, P.4    Bird, A.5    Reinberg, D.6
  • 9
    • 0036161439 scopus 로고    scopus 로고
    • Enzymatic activity associated wih calss-II HDACs is dependent on a mutiprotein complex containing HDAC3 and SMRT/N-CoR
    • Fischle W., Dequiedt F., Hendzel M.J., Guenther M.G., Lazar M.A., Voelter W., and Verdin E. Enzymatic activity associated wih calss-II HDACs is dependent on a mutiprotein complex containing HDAC3 and SMRT/N-CoR. Mol. Cell 9 (2002) 45-57
    • (2002) Mol. Cell , vol.9 , pp. 45-57
    • Fischle, W.1    Dequiedt, F.2    Hendzel, M.J.3    Guenther, M.G.4    Lazar, M.A.5    Voelter, W.6    Verdin, E.7
  • 10
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase-3
    • Guenther M.G., Barak O., and Lazar M.A. The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase-3. Mol. Cell. Biol. 21 (2001) 6091-6101
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6091-6101
    • Guenther, M.G.1    Barak, O.2    Lazar, M.A.3
  • 11
    • 0034192756 scopus 로고    scopus 로고
    • A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness
    • Guenther M.G., Lane W.S., Fischle W., Verdin E., Lazar M.A., and Shiekhatter R. A core SMRT corepressor complex containing HDAC3 and TBL1, a WD40-repeat protein linked to deafness. Genes Dev. 14 (2000) 1048-1057
    • (2000) Genes Dev. , vol.14 , pp. 1048-1057
    • Guenther, M.G.1    Lane, W.S.2    Fischle, W.3    Verdin, E.4    Lazar, M.A.5    Shiekhatter, R.6
  • 12
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 id an NAD-dependent histone-deacetylase
    • Imai S.I., Armstrong C.M., Kaeberlein M., and Guarente L. Transcriptional silencing and longevity protein Sir2 id an NAD-dependent histone-deacetylase. Nature 403 (2000) 795-800
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.I.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 14
    • 0034731501 scopus 로고    scopus 로고
    • Sds3 (suppressor of defective silencing-3) is an integral component of the yeast Sin3/Rpd3 histone deacetylase complex and is required for histone deacetylase activity
    • Lechner T., Carrozza M.J., Yu Y.X., Grant P.A., Eberharter A., Vannier D., Brosch G., Stillman D.J., Shore D., and Workman J.L. Sds3 (suppressor of defective silencing-3) is an integral component of the yeast Sin3/Rpd3 histone deacetylase complex and is required for histone deacetylase activity. J. Biol. Chem. 275 (2000) 40961-40966
    • (2000) J. Biol. Chem. , vol.275 , pp. 40961-40966
    • Lechner, T.1    Carrozza, M.J.2    Yu, Y.X.3    Grant, P.A.4    Eberharter, A.5    Vannier, D.6    Brosch, G.7    Stillman, D.J.8    Shore, D.9    Workman, J.L.10
  • 17
    • 0036097357 scopus 로고    scopus 로고
    • Cloning and expression of the gene for inorganic pyrophosphatase of Thermus caldophilus GK24 and properties of the enzyme
    • Hoe H.S., Jo I.G., Shin H.J., Kim H.K., Lee J.S., Kim Y.S., Lee D.S., and Kwon S.T. Cloning and expression of the gene for inorganic pyrophosphatase of Thermus caldophilus GK24 and properties of the enzyme. J. Microbiol. Biotechnol. 12 (2002) 301-305
    • (2002) J. Microbiol. Biotechnol. , vol.12 , pp. 301-305
    • Hoe, H.S.1    Jo, I.G.2    Shin, H.J.3    Kim, H.K.4    Lee, J.S.5    Kim, Y.S.6    Lee, D.S.7    Kwon, S.T.8
  • 18
    • 85010439719 scopus 로고
    • A procedure for isolation of deoxyribonucleic acid from micro-organism
    • Marmur J. A procedure for isolation of deoxyribonucleic acid from micro-organism. J. Mol. Biol. 3 (1961) 208-218
    • (1961) J. Mol. Biol. , vol.3 , pp. 208-218
    • Marmur, J.1
  • 19
    • 0032849859 scopus 로고    scopus 로고
    • CAP3: a DNA sequence assembly program
    • Huang X., and Madan A. CAP3: a DNA sequence assembly program. Genome Res. 9 (1999) 868-877
    • (1999) Genome Res. , vol.9 , pp. 868-877
    • Huang, X.1    Madan, A.2
  • 22
    • 0036042495 scopus 로고    scopus 로고
    • Histone deacetylases in Trypanosoma brucei: two are essential and another is required for normal cell cycle progression
    • Ingram A.K., and Horn D. Histone deacetylases in Trypanosoma brucei: two are essential and another is required for normal cell cycle progression. Mol. Microbiol. 45 (2002) 89-97
    • (2002) Mol. Microbiol. , vol.45 , pp. 89-97
    • Ingram, A.K.1    Horn, D.2
  • 23
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidal M., and Gaber R.F. RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol. Cell. Biol. 11 (1991) 6317-6327
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 6317-6327
    • Vidal, M.1    Gaber, R.F.2
  • 24
    • 0029822783 scopus 로고    scopus 로고
    • Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme
    • Sakurada K., Ohta T., Fujishiro K., Hasegawa M., and Aisaka K. Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme. J. Bacteriol. 178 (1996) 5781-5786
    • (1996) J. Bacteriol. , vol.178 , pp. 5781-5786
    • Sakurada, K.1    Ohta, T.2    Fujishiro, K.3    Hasegawa, M.4    Aisaka, K.5
  • 25
    • 0019287872 scopus 로고
    • Thermostability and aliphatic index of globular proteins
    • Ikai A. Thermostability and aliphatic index of globular proteins. J. Biochem. 88 (1980) 1895-1898
    • (1980) J. Biochem. , vol.88 , pp. 1895-1898
    • Ikai, A.1
  • 26
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 27
    • 0025612425 scopus 로고
    • Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence
    • Guruprasad K., Reddy B.V.B., and Pandit M.W. Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Eng. 4 (1990) 155-161
    • (1990) Protein Eng. , vol.4 , pp. 155-161
    • Guruprasad, K.1    Reddy, B.V.B.2    Pandit, M.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.