메뉴 건너뛰기




Volumn 47, Issue 5, 2008, Pages 1403-1413

The carboxy-terminal domain of xeroderma pigmentosum complementation group C protein, involved in TFIIH and centrin binding, is highly disordered

Author keywords

[No Author keywords available]

Indexed keywords

DNA DAMAGE; STRUCTURAL CHARACTERIZATION; XERODERMA PIGMENTOSUM;

EID: 38849204912     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701863u     Document Type: Article
Times cited : (11)

References (57)
  • 1
    • 0033118354 scopus 로고    scopus 로고
    • Molecular mechanism of nucleotide excision repair
    • de Laat, W. L., Jaspers, N. G. J., and Hoeijmakers, J. H. J. (1999) Molecular mechanism of nucleotide excision repair, Gen. Dev. 13, 768-785.
    • (1999) Gen. Dev , vol.13 , pp. 768-785
    • de Laat, W.L.1    Jaspers, N.G.J.2    Hoeijmakers, J.H.J.3
  • 3
    • 34247381126 scopus 로고    scopus 로고
    • An aromatic sensor with aversion to damaged strands confers versatility to DNA repair
    • Maillard, O., Solyom, S., and Naegeli, H. (2007) An aromatic sensor with aversion to damaged strands confers versatility to DNA repair, PLoS Biol. 5, e79.
    • (2007) PLoS Biol , vol.5
    • Maillard, O.1    Solyom, S.2    Naegeli, H.3
  • 4
    • 0025775473 scopus 로고
    • Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes
    • Venema, J., van Hoffen, A., Karcagi, V., Natarajan, A. T., van Zeeland, A. A., and Mullenders, L. H. F. (1991) Xeroderma pigmentosum complementation group C cells remove pyrimidine dimers selectively from the transcribed strand of active genes, Mol. Cell. Biol. 11, 4128-4134.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 4128-4134
    • Venema, J.1    van Hoffen, A.2    Karcagi, V.3    Natarajan, A.T.4    van Zeeland, A.A.5    Mullenders, L.H.F.6
  • 6
    • 20744446570 scopus 로고    scopus 로고
    • Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein
    • Nishi, R., Okuda, Y., Watanabe, E., Mori, T., Iwai, S., Masutani, C., Sugasawa, K., and Hanaoka, F. (2005) Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein, Mol. Cell Biol. 25, 5664-5674.
    • (2005) Mol. Cell Biol , vol.25 , pp. 5664-5674
    • Nishi, R.1    Okuda, Y.2    Watanabe, E.3    Mori, T.4    Iwai, S.5    Masutani, C.6    Sugasawa, K.7    Hanaoka, F.8
  • 8
    • 0034027382 scopus 로고    scopus 로고
    • Mutations in the XPC gene in families with Xeroderma Pigmentosum and consequences at the cell, protein, and transcription levels
    • Chavanne, F., Broughton, B. C., Pietra, D., Nardo, T., Browitt, A., lehmann, A. R., and Stefanini, M. (2000) Mutations in the XPC gene in families with Xeroderma Pigmentosum and consequences at the cell, protein, and transcription levels, Cancer Res. 60, 1974-1982.
    • (2000) Cancer Res , vol.60 , pp. 1974-1982
    • Chavanne, F.1    Broughton, B.C.2    Pietra, D.3    Nardo, T.4    Browitt, A.5    lehmann, A.R.6    Stefanini, M.7
  • 9
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by Rad4 nucleotide excision repair protein
    • Min, J.-H., and Pavletich, N. P. (2007) Recognition of DNA damage by Rad4 nucleotide excision repair protein, Nature 449, 570-575.
    • (2007) Nature , vol.449 , pp. 570-575
    • Min, J.-H.1    Pavletich, N.P.2
  • 10
    • 33845575990 scopus 로고    scopus 로고
    • Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein
    • Bunick, C. G., Miller, M. R., Fuller, B. E., Fanning, E., and Chazin, W. J. (2006) Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein, Biochemistry 45, 14965-14979.
    • (2006) Biochemistry , vol.45 , pp. 14965-14979
    • Bunick, C.G.1    Miller, M.R.2    Fuller, B.E.3    Fanning, E.4    Chazin, W.J.5
  • 12
    • 0037413689 scopus 로고    scopus 로고
    • Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase
    • Shimizu, Y., Iwai, S., Hanaoka, F., and Sugasawa, K. (2002) Xeroderma pigmentosum group C protein interacts physically and functionally with thymine DNA glycosylase, EMBO J. 22, 164-173.
    • (2002) EMBO J , vol.22 , pp. 164-173
    • Shimizu, Y.1    Iwai, S.2    Hanaoka, F.3    Sugasawa, K.4
  • 13
    • 0034737426 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor HH to dammaged DNA
    • Yokoi, M., Masutani, C., Maekawa, T., Sugasawa, K., Ohkuma, Y., and Hanaoka, F. (2000) The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor HH to dammaged DNA, J. Biol. Chem. 275, 9870-9875.
    • (2000) J. Biol. Chem , vol.275 , pp. 9870-9875
    • Yokoi, M.1    Masutani, C.2    Maekawa, T.3    Sugasawa, K.4    Ohkuma, Y.5    Hanaoka, F.6
  • 14
    • 0037150494 scopus 로고    scopus 로고
    • The carboxyterminal domain of XPC protein plays a crucial role in nucleotide excision repair trough interactions with transcription factor HH
    • Uchida, A., Sugasawa, K., Masutani, C., Dohmae, N., Araki, M., Yokoi, M., Ohkuma, Y., and Hanaoka, F. (2002) The carboxyterminal domain of XPC protein plays a crucial role in nucleotide excision repair trough interactions with transcription factor HH, DNA Repair 1, 449-461.
    • (2002) DNA Repair , vol.1 , pp. 449-461
    • Uchida, A.1    Sugasawa, K.2    Masutani, C.3    Dohmae, N.4    Araki, M.5    Yokoi, M.6    Ohkuma, Y.7    Hanaoka, F.8
  • 15
    • 33745868296 scopus 로고    scopus 로고
    • The structure of the human centrin 2-xeroderma pigmentosum group C protein complex
    • Thompson, J. R., Ryan, Z. C., Salisbury, J. L., and Kumar, R. (2006) The structure of the human centrin 2-xeroderma pigmentosum group C protein complex, J. Biol. Chem. 281, 18746-18752.
    • (2006) J. Biol. Chem , vol.281 , pp. 18746-18752
    • Thompson, J.R.1    Ryan, Z.C.2    Salisbury, J.L.3    Kumar, R.4
  • 17
    • 34250834316 scopus 로고    scopus 로고
    • High sensitivity of human centrin 2 toward radiolytical oxidation: C-terminal tyrosinyl residue as the main target
    • Blouquit, Y., Duchambon, P., Brun, E., Marco, S., Rusconi, F., and Sicard-Roselli, C. (2007) High sensitivity of human centrin 2 toward radiolytical oxidation: C-terminal tyrosinyl residue as the main target. Free Radic. Biol. Med. 43, 216-228.
    • (2007) Free Radic. Biol. Med , vol.43 , pp. 216-228
    • Blouquit, Y.1    Duchambon, P.2    Brun, E.3    Marco, S.4    Rusconi, F.5    Sicard-Roselli, C.6
  • 19
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressivemultiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Higgins, D., Thompson, J., Gibson, T., Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressivemultiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Higgins, D.1    Thompson, J.2    Gibson, T.3    Thompson, J.D.4    Higgins, D.G.5    Gibson, T.J.6
  • 21
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with expanded reference set
    • Sreerama, N., and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with expanded reference set, Anal. Biochem. 287, 252-260.
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 23
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria, J. Appl. Crystallogr. 25, 495-503.
    • (1992) J. Appl. Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 24
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V., and Koch, M. H. (2001) Determination of domain structure of proteins from X-ray solution scattering, Biophys. J. 80, 2946-2953.
    • (2001) Biophys. J , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 25
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov, M. V., and Svergun, D. I. (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data, Biophys. J. 89, 1237-1250.
    • (2005) Biophys. J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 27
    • 0036128797 scopus 로고    scopus 로고
    • Natively unfolded proteins: A point where biology waits for physics
    • Uversky, V. N. (2002) Natively unfolded proteins: a point where biology waits for physics, Protein Sci. 11, 735-756.
    • (2002) Protein Sci , vol.11 , pp. 735-756
    • Uversky, V.N.1
  • 28
    • 33748258328 scopus 로고    scopus 로고
    • A practical overview of protein disorder prediction methods
    • Ferren, F., Longhi, S., Canard, B., and Karlin, D. (2006) A practical overview of protein disorder prediction methods, Proteins 65, 1-14.
    • (2006) Proteins , vol.65 , pp. 1-14
    • Ferren, F.1    Longhi, S.2    Canard, B.3    Karlin, D.4
  • 29
    • 0141924869 scopus 로고    scopus 로고
    • Xeroderma pigmentosum group C protein possesses a high affinity binding site for human centrin 2 and calmodulin
    • Popescu, A., Miron, S., Blouquit, Y., Duchambon, P., and Craescu, C. T. (2003) Xeroderma pigmentosum group C protein possesses a high affinity binding site for human centrin 2 and calmodulin, J. Biol. Chem. 278, 40252-40261.
    • (2003) J. Biol. Chem , vol.278 , pp. 40252-40261
    • Popescu, A.1    Miron, S.2    Blouquit, Y.3    Duchambon, P.4    Craescu, C.T.5
  • 32
    • 0019873820 scopus 로고
    • Estimation of protein secondary structure from circular dichroism
    • Provencher, S. W., and Glöckner, J. (1981) Estimation of protein secondary structure from circular dichroism, Biochemistry 20, 33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 33
    • 0033562629 scopus 로고    scopus 로고
    • Analysing protein circular dichroism spectra for accurate secondary structures
    • Johnson, W. C. (1999) Analysing protein circular dichroism spectra for accurate secondary structures, Proteins: Struct. Funct. Genet. 35, 307-312.
    • (1999) Proteins: Struct. Funct. Genet , vol.35 , pp. 307-312
    • Johnson, W.C.1
  • 34
    • 0034669882 scopus 로고    scopus 로고
    • Why are "natively unfolded" proteins unstructured under physiological conditions?
    • Uversky, V., N., Gillespie, J., R., and Fink, A., L. (2000) Why are "natively unfolded" proteins unstructured under physiological conditions?, Proteins Struct. Funct. Genet. 41, 415-427.
    • (2000) Proteins Struct. Funct. Genet , vol.41 , pp. 415-427
    • Uversky, V.N.1    Gillespie, J.R.2    Fink, A.L.3
  • 35
    • 0032444658 scopus 로고    scopus 로고
    • Trifluoroethanol and colleagues:coslovents come of age. Recent studies with peptides and proteins
    • Buck, M. (1998) Trifluoroethanol and colleagues:coslovents come of age. Recent studies with peptides and proteins, Q. Rev. Biophys. 31, 297-355.
    • (1998) Q. Rev. Biophys , vol.31 , pp. 297-355
    • Buck, M.1
  • 36
    • 33846185994 scopus 로고    scopus 로고
    • Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function
    • Povey, J. F., Smales, C. M., Hassard, S. J., and Howard, M. J. (2007) Comparison of the effects of 2,2,2-trifluoroethanol on peptide and protein structure and function, J. Struct. Biol. 157, 329-338.
    • (2007) J. Struct. Biol , vol.157 , pp. 329-338
    • Povey, J.F.1    Smales, C.M.2    Hassard, S.J.3    Howard, M.J.4
  • 37
    • 0027484016 scopus 로고
    • Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation
    • Thomas, P. D., and Dill, K. A. (1993) Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation, Protein Sci. 2, 2050-2065.
    • (1993) Protein Sci , vol.2 , pp. 2050-2065
    • Thomas, P.D.1    Dill, K.A.2
  • 38
    • 0026768829 scopus 로고
    • Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin
    • Dyson, H. J., Merutka, G., Waltho, J. P., Lemer, R. A., and Wright, P. E. (1992) Folding of peptide fragments comprising the complete sequence of proteins. Models for initiation of protein folding. I. Myohemerythrin, J. Mol. Biol. 226, 795-817.
    • (1992) J. Mol. Biol , vol.226 , pp. 795-817
    • Dyson, H.J.1    Merutka, G.2    Waltho, J.P.3    Lemer, R.A.4    Wright, P.E.5
  • 39
    • 0033055898 scopus 로고    scopus 로고
    • Trifluoroethanol-induced conformational transitions of proteins: Insights gained from the differences between α-lactalbumin and ribonuclease A
    • Gast, K., Zirwer, D., Müller-Frohne, M., and Damaschun, G. (1999) Trifluoroethanol-induced conformational transitions of proteins: insights gained from the differences between α-lactalbumin and ribonuclease A, Prot. Sci. 8, 625-634.
    • (1999) Prot. Sci , vol.8 , pp. 625-634
    • Gast, K.1    Zirwer, D.2    Müller-Frohne, M.3    Damaschun, G.4
  • 40
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov, M. V., and Svergun, D. I. (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data, Biophys. J., 1237-1250.
    • (2005) Biophys. J , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 41
    • 0025299563 scopus 로고
    • Influence of the solvent on the conformational-dependent properties of random-coil polypeptides. I. The mean-square of the end-to-end distance and of the dipole moment
    • Rowe, G., and Lopez, A. (1990) Influence of the solvent on the conformational-dependent properties of random-coil polypeptides. I. The mean-square of the end-to-end distance and of the dipole moment, Biophys. Chem. 36, 57-64.
    • (1990) Biophys. Chem , vol.36 , pp. 57-64
    • Rowe, G.1    Lopez, A.2
  • 42
    • 10044296373 scopus 로고    scopus 로고
    • SAXS study of the PIR domain from the Grb14 molecular adaptor: A natively unfolded protein with a transient structure primer?
    • Moncoq, K., Broutin, I., Craescu, C. T., Vachette, P., Ducruix, A., and Durand, D. (2004) SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer? Biophys. J. 87, 4056-4064.
    • (2004) Biophys. J , vol.87 , pp. 4056-4064
    • Moncoq, K.1    Broutin, I.2    Craescu, C.T.3    Vachette, P.4    Ducruix, A.5    Durand, D.6
  • 43
    • 33645233083 scopus 로고    scopus 로고
    • Flexibility and Plasticity of Human Centrin 2 Binding to the Protein XPC from Nuclear Excision Repair
    • Yang, A., Miron, S., Mouawad, L., Duchambon, P., Blouquit, Y., and Craescu, C. T. (2006) Flexibility and Plasticity of Human Centrin 2 Binding to the Protein XPC from Nuclear Excision Repair, Biochemistry 45, 3653-3663.
    • (2006) Biochemistry , vol.45 , pp. 3653-3663
    • Yang, A.1    Miron, S.2    Mouawad, L.3    Duchambon, P.4    Blouquit, Y.5    Craescu, C.T.6
  • 44
    • 0028871798 scopus 로고
    • Side-chain conformational entropy in protein folding
    • Doig, A. J., and Sternberg, M. J. (1995) Side-chain conformational entropy in protein folding, Prot. Sci. 4, 2247-2251.
    • (1995) Prot. Sci , vol.4 , pp. 2247-2251
    • Doig, A.J.1    Sternberg, M.J.2
  • 45
    • 4344707281 scopus 로고    scopus 로고
    • Unfolded proteins and protein folding studied by NMR
    • Dyson, H. J., and Wright, P. E. (2004) Unfolded proteins and protein folding studied by NMR, Chem. Rev. 104, 3607-3622.
    • (2004) Chem. Rev , vol.104 , pp. 3607-3622
    • Dyson, H.J.1    Wright, P.E.2
  • 47
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink, A. L. (2005) Natively unfolded proteins, Curr. Opin. Struct. Biol. 15, 35-41.
    • (2005) Curr. Opin. Struct. Biol , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 48
    • 0036402827 scopus 로고    scopus 로고
    • Identification and functions of usefully disordered proteins
    • Dunker, A. K., Brown, C. J., and Obradovic, Z. (2002) Identification and functions of usefully disordered proteins, Adv. Prot. Chem. 62, 25-49.
    • (2002) Adv. Prot. Chem , vol.62 , pp. 25-49
    • Dunker, A.K.1    Brown, C.J.2    Obradovic, Z.3
  • 49
    • 0036468397 scopus 로고    scopus 로고
    • Coupling of folding and binding for unstructured proteins
    • Dyson, H. J., and Wright, P. E. (2002) Coupling of folding and binding for unstructured proteins, Curr. Opin. Struct. Biol. 12, 54-60.
    • (2002) Curr. Opin. Struct. Biol , vol.12 , pp. 54-60
    • Dyson, H.J.1    Wright, P.E.2
  • 50
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the Xeroderma Pigmentosum group C complex that initiates global genome nucleotide excision repair
    • Araki, M., Masutani, C., Takemura, M., Uchida, A., Sugasawa, K., Kondoh, J., Ohkuma, Y., and Hanaoka, F. (2001) Centrosome protein centrin 2/caltractin 1 is part of the Xeroderma Pigmentosum group C complex that initiates global genome nucleotide excision repair, J. Biol. Chem. 276, 18665-18672.
    • (2001) J. Biol. Chem , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 52
    • 33645988522 scopus 로고    scopus 로고
    • Conserved XPB core structure and motifs for DNA un winding: Implications for pathway selection of transcription or excision repair
    • Fan, L., Arvai, A. S., Cooper, P. K., Iwai, S., Hanaoka, F., and Tainer, J. A. (2006) Conserved XPB core structure and motifs for DNA un winding: implications for pathway selection of transcription or excision repair, Mol. Cell 22, 27-37.
    • (2006) Mol. Cell , vol.22 , pp. 27-37
    • Fan, L.1    Arvai, A.S.2    Cooper, P.K.3    Iwai, S.4    Hanaoka, F.5    Tainer, J.A.6
  • 54
    • 33645292569 scopus 로고    scopus 로고
    • Calmodulin signaling: Analysis and prediction of a disorder-dependent molecular recognition
    • Radivojac, P., Vucetic, S., O'Connor, T. R., Uversky, V. N., Obradovic, Z., and Dunker, A. K. (2006) Calmodulin signaling: analysis and prediction of a disorder-dependent molecular recognition, Proteins 63, 398-410.
    • (2006) Proteins , vol.63 , pp. 398-410
    • Radivojac, P.1    Vucetic, S.2    O'Connor, T.R.3    Uversky, V.N.4    Obradovic, Z.5    Dunker, A.K.6
  • 55
    • 0037155689 scopus 로고    scopus 로고
    • Calmodulin in action: Diversity in target recognition and activation mechanisms
    • Hoeflich, K. P., and Ikura, M. (2002) Calmodulin in action: diversity in target recognition and activation mechanisms, Cell 108, 739-742.
    • (2002) Cell , vol.108 , pp. 739-742
    • Hoeflich, K.P.1    Ikura, M.2
  • 56
    • 0035102950 scopus 로고    scopus 로고
    • Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome
    • Araujo, S. J., Nigg, E. A., and Woody, R. W. (2001) Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome, Mol. Cell Biol. 21, 2281-2291.
    • (2001) Mol. Cell Biol , vol.21 , pp. 2281-2291
    • Araujo, S.J.1    Nigg, E.A.2    Woody, R.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.