메뉴 건너뛰기




Volumn 47, Issue 25, 2008, Pages 6519-6530

The thymine-DNA glycosylase regulatory domain: Residual structure and DNA binding

Author keywords

[No Author keywords available]

Indexed keywords

AMERICAN CHEMICAL SOCIETY (ACS); BASE EXCISION REPAIR (BER); CATALYTIC CORE; CATALYTIC DOMAINS; DEGREE OF ORGANIZATION; DNA GLYCOSYLASE; DNA GLYCOSYLASES; DNA METHYLTRANSFERASE (DNMT); DNA-BINDING; DOUBLE-STRANDED DNA (DS-DNA); ENZYMATIC DEAMINATION; EPIGENETIC REGULATION; FUNCTIONAL REGULATION; HIGH-FREQUENCY (HF); MOLECULAR FUNCTIONS; N-TERMINAL REGION; NUCLEAR RECEPTORS; POSTTRANSLATIONAL MODIFICATION (PTM); PROCESSING ACTIVITY; REGULATORY DOMAINS; REGULATORY FUNCTIONS; RESIDUAL STRUCTURE; THREE-DIMENSIONAL (3D) STRUCTURING; TRANSCRIPTION REGULATIONS; TRANSCRIPTIONAL COREGULATORS;

EID: 45749124759     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7022283     Document Type: Article
Times cited : (39)

References (40)
  • 1
    • 0034576553 scopus 로고    scopus 로고
    • The alpha/beta fold uracil DNA glycosylases: A common origin with diverse fates
    • RESEARCH0007
    • Aravind, L., and Koonin, E. V. (2000) The alpha/beta fold uracil DNA glycosylases: a common origin with diverse fates. Genome Biol. 1, (RESEARCH0007).
    • (2000) Genome Biol , vol.1
    • Aravind, L.1    Koonin, E.V.2
  • 2
    • 24044460415 scopus 로고    scopus 로고
    • DNA base damage recognition and removal: New twists and grooves
    • Huffman, J. L., Sundheim, O., and Tainer, J. A. (2005) DNA base damage recognition and removal: new twists and grooves. Mutat. Res. 577, 55-76.
    • (2005) Mutat. Res , vol.577 , pp. 55-76
    • Huffman, J.L.1    Sundheim, O.2    Tainer, J.A.3
  • 3
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • Mol, C. D., Arvai, A. S., Slupphaug, G., Kavli, B., Alseth, I., Krokan, H. E., and Tainer, J. A. (1995) Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 80, 869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 4
    • 0037115911 scopus 로고    scopus 로고
    • Uracil in DNA-occurrence, consequences and repair
    • Krokan, H. E., Drablos, F., and Slupphaug, G. (2002) Uracil in DNA-occurrence, consequences and repair. Oncogene 21, 8935-8948.
    • (2002) Oncogene , vol.21 , pp. 8935-8948
    • Krokan, H.E.1    Drablos, F.2    Slupphaug, G.3
  • 5
    • 0025268279 scopus 로고
    • Spontaneous deamination of cytosine and 5-methylcytosine residues in DNA and replacement of 5-methylcytosine residues with cytosine residues
    • Ehrlich, M., Zhang, X. Y., and Inamdar, N. M. (1990) Spontaneous deamination of cytosine and 5-methylcytosine residues in DNA and replacement of 5-methylcytosine residues with cytosine residues. Mutat. Res. 238, 277-286.
    • (1990) Mutat. Res , vol.238 , pp. 277-286
    • Ehrlich, M.1    Zhang, X.Y.2    Inamdar, N.M.3
  • 6
    • 0034086023 scopus 로고    scopus 로고
    • Thymine-DNA glycosylase and G to A transition mutations at CpG sites
    • Waters, T. R., and Swann, P. F. (2000) Thymine-DNA glycosylase and G to A transition mutations at CpG sites. Mutat. Res. 462, 137-147.
    • (2000) Mutat. Res , vol.462 , pp. 137-147
    • Waters, T.R.1    Swann, P.F.2
  • 7
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G·T/U mismatch-specific DNA glycosylase: Mismatch recognition by complementary-strand interactions
    • Barrett, T. E., Savva, R., Panayotou, G., Barlow, T., Brown, T., Jiricny, J., and Pearl, L. H. (1998) Crystal structure of a G·T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92, 117-129.
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Jiricny, J.6    Pearl, L.H.7
  • 10
    • 0027383758 scopus 로고
    • The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells
    • Neddermann, P., and Jiricny, J. (1993) The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells. J. Biol. Chem. 268, 21218-21224.
    • (1993) J. Biol. Chem , vol.268 , pp. 21218-21224
    • Neddermann, P.1    Jiricny, J.2
  • 11
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
    • Hendrich, B., Hardeland, U., Ng, H. H., Jiricny, J., and Bird, A. (1999) The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature 401, 301-304.
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.H.3    Jiricny, J.4    Bird, A.5
  • 12
    • 0036305835 scopus 로고    scopus 로고
    • Structure and activity of a thermostable thymine-DNA glycosylase: Evidence for base twisting to remove mismatched normal DNA bases
    • Mol, C. D., Arvai, A. S., Begley, T. J., Cunningham, R. P., and Tainer, J. A. (2002) Structure and activity of a thermostable thymine-DNA glycosylase: evidence for base twisting to remove mismatched normal DNA bases. J. Mol. Biol. 315, 373-384.
    • (2002) J. Mol. Biol , vol.315 , pp. 373-384
    • Mol, C.D.1    Arvai, A.S.2    Begley, T.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 13
    • 0029805081 scopus 로고    scopus 로고
    • A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase
    • Gallinari, P., and Jiricny, J. (1996) A new class of uracil-DNA glycosylases related to human thymine-DNA glycosylase. Nature 383, 735-738.
    • (1996) Nature , vol.383 , pp. 735-738
    • Gallinari, P.1    Jiricny, J.2
  • 16
    • 0034721829 scopus 로고    scopus 로고
    • Separating substrate recognition from base hydrolysis in human thymine DNA glycosylase by mutational analysis
    • Hardeland, U., Bentele, M., Jiricny, J., and Schar, P. (2000) Separating substrate recognition from base hydrolysis in human thymine DNA glycosylase by mutational analysis. J. Biol. Chem. 275, 33449-33456.
    • (2000) J. Biol. Chem , vol.275 , pp. 33449-33456
    • Hardeland, U.1    Bentele, M.2    Jiricny, J.3    Schar, P.4
  • 17
    • 0034734383 scopus 로고    scopus 로고
    • Structure and function in the uracil-DNA glycosylase superfamily
    • Pearl, L. H. (2000) Structure and function in the uracil-DNA glycosylase superfamily. Mutat. Res. 460, 165-181.
    • (2000) Mutat. Res , vol.460 , pp. 165-181
    • Pearl, L.H.1
  • 18
    • 0038475941 scopus 로고    scopus 로고
    • Mismatch repair in methylated DNA. Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4
    • Wu, P., Qiu, C., Sohail, A., Zhang, X., Bhagwat, A. S., and Cheng, X. (2003) Mismatch repair in methylated DNA. Structure and activity of the mismatch-specific thymine glycosylase domain of methyl-CpG-binding protein MBD4. J. Biol. Chem. 278, 5285-5291.
    • (2003) J. Biol. Chem , vol.278 , pp. 5285-5291
    • Wu, P.1    Qiu, C.2    Sohail, A.3    Zhang, X.4    Bhagwat, A.S.5    Cheng, X.6
  • 19
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation
    • Steinacher, R., and Schar, P. (2005) Functionality of human thymine DNA glycosylase requires SUMO-regulated changes in protein conformation. Curr. Biol. 15, 616-623.
    • (2005) Curr. Biol , vol.15 , pp. 616-623
    • Steinacher, R.1    Schar, P.2
  • 20
    • 17144379416 scopus 로고    scopus 로고
    • SUMO modification: Wrestling with protein conformation
    • Ulrich, H. D. (2005) SUMO modification: wrestling with protein conformation. Curr. Biol. 15, R257-R259.
    • (2005) Curr. Biol , vol.15
    • Ulrich, H.D.1
  • 21
    • 0032516887 scopus 로고    scopus 로고
    • Retinoic acid receptors interact physically and functionally with the T:G mismatch-specific thymine-DNA glycosylase
    • Um, S., Harbers, M., Benecke, A., Pierrat, B., Losson, R., and Chambon, P. (1998) Retinoic acid receptors interact physically and functionally with the T:G mismatch-specific thymine-DNA glycosylase. J. Biol. Chem. 273, 20728-20736.
    • (1998) J. Biol. Chem , vol.273 , pp. 20728-20736
    • Um, S.1    Harbers, M.2    Benecke, A.3    Pierrat, B.4    Losson, R.5    Chambon, P.6
  • 22
  • 24
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • Tini, M., Benecke, A., Um, S. J., Torchia, J., Evans, R. M., and Chambon, P. (2002) Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription. Mol. Cell 9, 265-277.
    • (2002) Mol. Cell , vol.9 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.J.3    Torchia, J.4    Evans, R.M.5    Chambon, P.6
  • 25
    • 33846909036 scopus 로고    scopus 로고
    • Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair
    • Li, Y.-Q., Zhou, P.-Z., Zheng, X.-D., Walsh, C. P., and Xu, G.-L. (2007) Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair. Nucleic Acids Res. 35, 390-400.
    • (2007) Nucleic Acids Res , vol.35 , pp. 390-400
    • Li, Y.-Q.1    Zhou, P.-Z.2    Zheng, X.-D.3    Walsh, C.P.4    Xu, G.-L.5
  • 26
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • Hardeland, U., Steinacher, R., Jiricny, J., and Schar, P. (2002) Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J. 21, 1456-1464.
    • (2002) EMBO J , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 27
    • 33845733594 scopus 로고    scopus 로고
    • SUMO-1 dependent allosteric regulation of Thymine DNA Glycosylase alters subnuclear localization and CBP/p300 recruitment
    • Mohan, R. D., Rao, A., Gagliardi, J., and Tini, M. (2007) SUMO-1 dependent allosteric regulation of Thymine DNA Glycosylase alters subnuclear localization and CBP/p300 recruitment. Mol. Cell. Biol. 27, 229-243.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 229-243
    • Mohan, R.D.1    Rao, A.2    Gagliardi, J.3    Tini, M.4
  • 28
    • 14044278774 scopus 로고    scopus 로고
    • Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein
    • Takahashi, H., Hatakeyama, S., Saitoh, H., and Nakayama, K. I. (2005) Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. J. Biol. Chem. 280, 5611-5621.
    • (2005) J. Biol. Chem , vol.280 , pp. 5611-5621
    • Takahashi, H.1    Hatakeyama, S.2    Saitoh, H.3    Nakayama, K.I.4
  • 30
    • 0347087450 scopus 로고    scopus 로고
    • Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites
    • Lippens, G., Wieruszeski, J. M., Leroy, A., Smet, C., Sillen, A., Buee, L., and Landrieu, I. (2004) Proline-directed random-coil chemical shift values as a tool for the NMR assignment of the tau phosphorylation sites. ChemBioChem 5, 73-78.
    • (2004) ChemBioChem , vol.5 , pp. 73-78
    • Lippens, G.1    Wieruszeski, J.M.2    Leroy, A.3    Smet, C.4    Sillen, A.5    Buee, L.6    Landrieu, I.7
  • 31
    • 10844292609 scopus 로고    scopus 로고
    • Accepting its random coil nature allows a partial NMR assignment of the neuronal tau protein
    • Smet, C., Leroy, A., Sillen, A., Wieruszeski, J. M., Landrieu, I., and Lippens, G. (2004) Accepting its random coil nature allows a partial NMR assignment of the neuronal tau protein. ChemBioChem 5, 1639-1646.
    • (2004) ChemBioChem , vol.5 , pp. 1639-1646
    • Smet, C.1    Leroy, A.2    Sillen, A.3    Wieruszeski, J.M.4    Landrieu, I.5    Lippens, G.6
  • 32
    • 12044259775 scopus 로고    scopus 로고
    • 15N-enriched proteins. J. Am. Chem. Soc. 115, 7772-7777.
    • 15N-enriched proteins. J. Am. Chem. Soc. 115, 7772-7777.
  • 33
    • 0000208289 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects. J. Biomol. NMR 5, 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 34
    • 0026597879 scopus 로고
    • The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1992) The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 35
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: Implications for fibrillation
    • Marsh, J. A., Singh, V. K., Jia, Z., and Forman-Kay, J. D. (2006) Sensitivity of secondary structure propensities to sequence differences between alpha- and gamma-synuclein: implications for fibrillation. Protein Sci. 15, 2795-2804.
    • (2006) Protein Sci , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 36
    • 0032528013 scopus 로고    scopus 로고
    • Sequence requirements for stabilization of a peptide reverse turn in water solution. Proline is not essential for stability
    • Dyson, H. J., Bolinger, L., Feher, V. A., Osterhout, J. J., Jr., Yao, J., and Wright, P. E. (1998) Sequence requirements for stabilization of a peptide reverse turn in water solution. Proline is not essential for stability. Protein Sci. 255, 462-471.
    • (1998) Protein Sci , vol.255 , pp. 462-471
    • Dyson, H.J.1    Bolinger, L.2    Feher, V.A.3    Osterhout Jr., J.J.4    Yao, J.5    Wright, P.E.6
  • 37
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
    • Schwarzinger, S., Kroon, G. J., Foss, T. R., Wright, P. E., and Dyson, H. J. (2000) Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView. J. Biomol. NMR 18, 43-48.
    • (2000) J. Biomol. NMR , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 39
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: Preferential hydration in glycerol-water mixtures
    • Gekko, K., and Timasheff, S. N. (1981) Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20, 4667-4676.
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.