메뉴 건너뛰기




Volumn 9, Issue 6, 2010, Pages 700-707

Functional analysis of MUTYH mutated proteins associated with familial adenomatous polyposis

Author keywords

Base excision repair; DNA glycosylase assay; MUTYH; MUTYH mutants; MUTYH associated polyposis; Surface plasmon resonance

Indexed keywords

8 HYDROXYGUANINE; ADENINE; DNA GLYCOSYLASE MUTY; DNA POLYMERASE; GUANINE; THYMINE; 8-HYDROXYGUANINE; DNA; DNA GLYCOSYLTRANSFERASE; MALTOSE BINDING PROTEIN; MUTANT PROTEIN; PERIPLASMIC BINDING PROTEIN;

EID: 77952582935     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2010.03.008     Document Type: Article
Times cited : (40)

References (43)
  • 1
    • 10944251591 scopus 로고    scopus 로고
    • Repair and genetic consequences of endogeneous DNA base damage in mammalian cells
    • Barnes D.E., and Lindahl T. Repair and genetic consequences of endogeneous DNA base damage in mammalian cells. Annu. Rev. Genet. 38 (2004) 445-476
    • (2004) Annu. Rev. Genet. , vol.38 , pp. 445-476
    • Barnes, D.E.1    Lindahl, T.2
  • 2
    • 33847625356 scopus 로고    scopus 로고
    • Base damage and single-strand break repair: mechanisms and functional significance of short and long-patch repair subpathways
    • Fortini P., and Dogliotti E. Base damage and single-strand break repair: mechanisms and functional significance of short and long-patch repair subpathways. DNA Repair 6 (2006) 398-409
    • (2006) DNA Repair , vol.6 , pp. 398-409
    • Fortini, P.1    Dogliotti, E.2
  • 3
    • 0242383485 scopus 로고    scopus 로고
    • Human MutY: gene structure, protein functions and interactions, and role in carcinogenesis
    • Parker A.R., and Eshleman J.R. Human MutY: gene structure, protein functions and interactions, and role in carcinogenesis. Cell. Mol. Life Sci. 60 (2003) 2064-2083
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2064-2083
    • Parker, A.R.1    Eshleman, J.R.2
  • 4
    • 33845407758 scopus 로고    scopus 로고
    • Different DNA repair strategies to combat the threat from 8-oxoguanine
    • Russo M.T., De Luca G., Degan P., and Bignami M. Different DNA repair strategies to combat the threat from 8-oxoguanine. Mutat. Res. 614 (2007) 69-76
    • (2007) Mutat. Res. , vol.614 , pp. 69-76
    • Russo, M.T.1    De Luca, G.2    Degan, P.3    Bignami, M.4
  • 5
    • 0035253515 scopus 로고    scopus 로고
    • Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch
    • Yang H., Clendenin W.M., Wong D., Demple B., Slupska M.M., Chiang J.H., and Miller J.H. Enhanced activity of adenine-DNA glycosylase (Myh) by apurinic/apyrimidinic endonuclease (Ape1) in mammalian base excision repair of an A/GO mismatch. Nucleic Acids Res. 29 (2001) 743-752
    • (2001) Nucleic Acids Res. , vol.29 , pp. 743-752
    • Yang, H.1    Clendenin, W.M.2    Wong, D.3    Demple, B.4    Slupska, M.M.5    Chiang, J.H.6    Miller, J.H.7
  • 6
    • 10244255214 scopus 로고    scopus 로고
    • Futile short-patch DNA base excision repair of adenine:8-oxoguanine mispair
    • Hashimoto K., Tominaga Y., Nakabeppu Y., and Moriya M. Futile short-patch DNA base excision repair of adenine:8-oxoguanine mispair. Nucleic Acids Res. 32 (2004) 5928-5934
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5928-5934
    • Hashimoto, K.1    Tominaga, Y.2    Nakabeppu, Y.3    Moriya, M.4
  • 7
    • 2642532610 scopus 로고    scopus 로고
    • Aphidicolin-resistant and -sensitive base excision repair in wild-type and DNA polymerase beta-defective mouse cells
    • Parlanti E., Pascucci B., Terrados G., Blanco L., and Dogliotti E. Aphidicolin-resistant and -sensitive base excision repair in wild-type and DNA polymerase beta-defective mouse cells. DNA Repair 3 (2004) 703-710
    • (2004) DNA Repair , vol.3 , pp. 703-710
    • Parlanti, E.1    Pascucci, B.2    Terrados, G.3    Blanco, L.4    Dogliotti, E.5
  • 8
    • 70849113575 scopus 로고    scopus 로고
    • An 8-oxo-guanine repair pathway coordinated by MUTYH glycosylase and DNA polymerase lambda
    • van Loon B., and Hübscher U. An 8-oxo-guanine repair pathway coordinated by MUTYH glycosylase and DNA polymerase lambda. Proc. Natl. Acad. Sci. U.S.A. 106 (2009) 18201-18206
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 18201-18206
    • van Loon, B.1    Hübscher, U.2
  • 9
    • 0037192812 scopus 로고    scopus 로고
    • Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6
    • Gu Y., Parker A., Wilson T.M., Bai H., Chang D.Y., and Lu A.L. Human MutY homolog, a DNA glycosylase involved in base excision repair, physically and functionally interacts with mismatch repair proteins human MutS homolog 2/human MutS homolog 6. J. Biol. Chem. 277 (2002) 11135-11142
    • (2002) J. Biol. Chem. , vol.277 , pp. 11135-11142
    • Gu, Y.1    Parker, A.2    Wilson, T.M.3    Bai, H.4    Chang, D.Y.5    Lu, A.L.6
  • 10
    • 0035937102 scopus 로고    scopus 로고
    • Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair
    • Parker A., Gu Y., Mahoney W., Lee S.H., Singh K.K., and Lu A.L. Human homolog of the MutY repair protein (hMYH) physically interacts with proteins involved in long patch DNA base excision repair. J. Biol. Chem. 276 (2001) 5547-5555
    • (2001) J. Biol. Chem. , vol.276 , pp. 5547-5555
    • Parker, A.1    Gu, Y.2    Mahoney, W.3    Lee, S.H.4    Singh, K.K.5    Lu, A.L.6
  • 11
    • 0030004207 scopus 로고    scopus 로고
    • Cloning and sequencing a human homolog (hMYH) of the Escherichia coli MutY gene whose function is required for the repair of oxidative DNA damage
    • Slupska M.M., Baikalov C., Luther W.M., Chiang J.H., Wie Y.F., and Miller J.H. Cloning and sequencing a human homolog (hMYH) of the Escherichia coli MutY gene whose function is required for the repair of oxidative DNA damage. J. Bacteriol. 178 (1996) 3885-3892
    • (1996) J. Bacteriol. , vol.178 , pp. 3885-3892
    • Slupska, M.M.1    Baikalov, C.2    Luther, W.M.3    Chiang, J.H.4    Wie, Y.F.5    Miller, J.H.6
  • 12
    • 0034671587 scopus 로고    scopus 로고
    • Adenine excisional repair function of MYH protein on the adenine: 8-hydroxyguanine base pair in double-stranded DNA
    • Shinmura K., Yamaguchi S., Saitoh T., Takeuchi-Sasaki M., Kim S.R., Nohmi T., and Yokota J. Adenine excisional repair function of MYH protein on the adenine: 8-hydroxyguanine base pair in double-stranded DNA. Nucleic Acids Res. 28 (2000) 4912-4918
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4912-4918
    • Shinmura, K.1    Yamaguchi, S.2    Saitoh, T.3    Takeuchi-Sasaki, M.4    Kim, S.R.5    Nohmi, T.6    Yokota, J.7
  • 13
    • 0034654256 scopus 로고    scopus 로고
    • Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria
    • Ohtsubo T., Nishioka K., Imaiso Y., Iwai S., Shimokawa H., Oda H., Fujiwara T., and Nakabeppu Y. Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multiple forms of hMYH located in nuclei and mitochondria. Nucleic Acids Res. 28 (2000) 1355-1364
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1355-1364
    • Ohtsubo, T.1    Nishioka, K.2    Imaiso, Y.3    Iwai, S.4    Shimokawa, H.5    Oda, H.6    Fujiwara, T.7    Nakabeppu, Y.8
  • 14
    • 0036297160 scopus 로고    scopus 로고
    • Characterization of 2-hydroxyadenine DNA glycosylase activity of Escherichia coli MutY protein
    • Hashiguchi K., Zhang Q.M., Sugiyama H., Ikeda H.S., and Yonei S. Characterization of 2-hydroxyadenine DNA glycosylase activity of Escherichia coli MutY protein. Int. J. Radiat. Biol. 78 (2002) 585-592
    • (2002) Int. J. Radiat. Biol. , vol.78 , pp. 585-592
    • Hashiguchi, K.1    Zhang, Q.M.2    Sugiyama, H.3    Ikeda, H.S.4    Yonei, S.5
  • 15
    • 13844313936 scopus 로고    scopus 로고
    • A functional analysis of the DNA glycosylase activity of mouse MUTYH protein excising 2-hydroxyadenine opposite guanine in DNA
    • Ushijima Y., Tominaga Y., Miura T., Tsuchimoto D., Sakumi K., and Nakabeppu Y. A functional analysis of the DNA glycosylase activity of mouse MUTYH protein excising 2-hydroxyadenine opposite guanine in DNA. Nucleic Acids Res. 33 (2005) 672-682
    • (2005) Nucleic Acids Res. , vol.33 , pp. 672-682
    • Ushijima, Y.1    Tominaga, Y.2    Miura, T.3    Tsuchimoto, D.4    Sakumi, K.5    Nakabeppu, Y.6
  • 18
    • 0023992806 scopus 로고
    • The mutY gene: a mutator locus in Escherichia coli that generates GC:TA transversions
    • Nghiem Y., Cabrera M., Cupples C.G., and Miller J.H. The mutY gene: a mutator locus in Escherichia coli that generates GC:TA transversions. Proc. Natl. Acad. Sci. U.S.A. 85 (1988) 2709-2713
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 2709-2713
    • Nghiem, Y.1    Cabrera, M.2    Cupples, C.G.3    Miller, J.H.4
  • 22
    • 33847333956 scopus 로고    scopus 로고
    • MUTYH-associated polyposis-from defect in base excision repair to clinical genetic testing
    • Cheadle J.P., and Sampson J.R. MUTYH-associated polyposis-from defect in base excision repair to clinical genetic testing. DNA Repair 6 (2007) 274-279
    • (2007) DNA Repair , vol.6 , pp. 274-279
    • Cheadle, J.P.1    Sampson, J.R.2
  • 24
    • 0037459233 scopus 로고    scopus 로고
    • Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E. coli enzymes
    • Chmiel N.H., Livingston A.L., and David S.S. Insight into the functional consequences of inherited variants of the hMYH adenine glycosylase associated with colorectal cancer: complementation assays with hMYH variants and pre-steady-state kinetics of the corresponding mutated E. coli enzymes. J. Mol. Biol. 327 (2003) 431-443
    • (2003) J. Mol. Biol. , vol.327 , pp. 431-443
    • Chmiel, N.H.1    Livingston, A.L.2    David, S.S.3
  • 25
    • 48549095660 scopus 로고    scopus 로고
    • Characterization of mutant MUTYH proteins associated with familial colorectal cancer
    • Ali M., Kim H., Cleary S., Cupples C., Gallinger S., and Bristow R. Characterization of mutant MUTYH proteins associated with familial colorectal cancer. Gastroenterology 135 (2008) 499-507
    • (2008) Gastroenterology , vol.135 , pp. 499-507
    • Ali, M.1    Kim, H.2    Cleary, S.3    Cupples, C.4    Gallinger, S.5    Bristow, R.6
  • 26
    • 1242338775 scopus 로고    scopus 로고
    • Identification of critical residues required for the mutation avoidance function of human MutY (hMYH) and implications in colorectal cancer
    • Wooden S.H., Bassett H.M., Wood T.G., and McCullough A.K. Identification of critical residues required for the mutation avoidance function of human MutY (hMYH) and implications in colorectal cancer. Cancer Lett. 205 (2004) 89-95
    • (2004) Cancer Lett. , vol.205 , pp. 89-95
    • Wooden, S.H.1    Bassett, H.M.2    Wood, T.G.3    McCullough, A.K.4
  • 27
    • 12344258702 scopus 로고    scopus 로고
    • Insight into the functional consequences of hMYH variants associated with colorectal cancer: distinct differences in the adenine glycosylase activity and the response to AP endonucleases of Y150C and G365D murine MYH
    • Pope M.A., Chmiel N., and David S.S. Insight into the functional consequences of hMYH variants associated with colorectal cancer: distinct differences in the adenine glycosylase activity and the response to AP endonucleases of Y150C and G365D murine MYH. DNA Repair 4 (2005) 315-325
    • (2005) DNA Repair , vol.4 , pp. 315-325
    • Pope, M.A.1    Chmiel, N.2    David, S.S.3
  • 28
    • 13744261252 scopus 로고    scopus 로고
    • Functional characterization of two human MutY homolog (hMYH) missense mutations (R227 and V232F) that lie within the putative hMSH6 binding domain and are associated with MYH polyposis
    • Bai H., Jones S., Guan X., Wilson T.M., Sampson J.R., Cheadle J.P., and Lu A.L. Functional characterization of two human MutY homolog (hMYH) missense mutations (R227 and V232F) that lie within the putative hMSH6 binding domain and are associated with MYH polyposis. Nucleic Acids Res. 33 (2005) 597-604
    • (2005) Nucleic Acids Res. , vol.33 , pp. 597-604
    • Bai, H.1    Jones, S.2    Guan, X.3    Wilson, T.M.4    Sampson, J.R.5    Cheadle, J.P.6    Lu, A.L.7
  • 30
    • 33947580840 scopus 로고    scopus 로고
    • Functional characterization of human MutY homolog (hMYH) missense mutation (R231L) that is linked with hMYH-associated polyposis
    • Bai S., Grist J., Gardner G., Suthers G., Wilson T.M., and Lu A.L. Functional characterization of human MutY homolog (hMYH) missense mutation (R231L) that is linked with hMYH-associated polyposis. Cancer Lett. 250 (2007) 74-81
    • (2007) Cancer Lett. , vol.250 , pp. 74-81
    • Bai, S.1    Grist, J.2    Gardner, G.3    Suthers, G.4    Wilson, T.M.5    Lu, A.L.6
  • 32
    • 67649118180 scopus 로고    scopus 로고
    • Surface plasmon resonance assay of DNA-protein interactions
    • Stockley P.G., and Persson B. Surface plasmon resonance assay of DNA-protein interactions. Methods Mol. Biol. 543 (2009) 653-669
    • (2009) Methods Mol. Biol. , vol.543 , pp. 653-669
    • Stockley, P.G.1    Persson, B.2
  • 34
    • 70149108748 scopus 로고    scopus 로고
    • Excised damaged base determines the turnover of human N-methylpurine-DNA glycosylase
    • Adhikari S., Uren A., and Roy R. Excised damaged base determines the turnover of human N-methylpurine-DNA glycosylase. DNA Repair 8 (2009) 1201-1206
    • (2009) DNA Repair , vol.8 , pp. 1201-1206
    • Adhikari, S.1    Uren, A.2    Roy, R.3
  • 36
    • 0032553004 scopus 로고    scopus 로고
    • Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates
    • Porello S.L., Leyes A.E., and David S.S. Single-turnover and pre-steady-state kinetics of the reaction of the adenine glycosylase MutY with mismatch-containing DNA substrates. Biochemistry 37 (1998) 14756-14764
    • (1998) Biochemistry , vol.37 , pp. 14756-14764
    • Porello, S.L.1    Leyes, A.E.2    David, S.S.3
  • 37
    • 70450224248 scopus 로고    scopus 로고
    • Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associates with colorectal cancer
    • Kundu S., Brinkmeyer M.K., Livingston A.L., and David S.S. Adenine removal activity and bacterial complementation with the human MutY homologue (MUTYH) and Y165C, G382D, P391L and Q324R variants associates with colorectal cancer. DNA Repair 8 (2009) 1400-1410
    • (2009) DNA Repair , vol.8 , pp. 1400-1410
    • Kundu, S.1    Brinkmeyer, M.K.2    Livingston, A.L.3    David, S.S.4
  • 39
    • 0033580647 scopus 로고    scopus 로고
    • The C-terminal domain of the adenine-DNA glycosylase MutY confers specificity for 8-oxoguanine, adenine mispairs and may have evolved from MutT, an 8-oxo-dGTPase
    • Noll D.M., Gogos A., Granek J.A., and Clarke N.D. The C-terminal domain of the adenine-DNA glycosylase MutY confers specificity for 8-oxoguanine, adenine mispairs and may have evolved from MutT, an 8-oxo-dGTPase. Biochemistry 38 (1999) 6374-6379
    • (1999) Biochemistry , vol.38 , pp. 6374-6379
    • Noll, D.M.1    Gogos, A.2    Granek, J.A.3    Clarke, N.D.4
  • 40
    • 0038578040 scopus 로고    scopus 로고
    • The C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities
    • Li L., and Lu A.L. The C-terminal domain of Escherichia coli MutY is involved in DNA binding and glycosylase activities. Nucleic Acids Res. 31 (2003) 3038-3049
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3038-3049
    • Li, L.1    Lu, A.L.2
  • 41
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • Fromme J.C., Banerjee A., Huang S.J., and Verdine G. Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase. Nature 427 (2004) 652-656
    • (2004) Nature , vol.427 , pp. 652-656
    • Fromme, J.C.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.4
  • 42
    • 7944228647 scopus 로고    scopus 로고
    • DNA damage recognition and repair by the murine MutY homologue
    • Pope M.A., and David S.S. DNA damage recognition and repair by the murine MutY homologue. DNA Repair 4 (2005) 91-102
    • (2005) DNA Repair , vol.4 , pp. 91-102
    • Pope, M.A.1    David, S.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.