메뉴 건너뛰기




Volumn 1672, Issue 3, 2004, Pages 174-183

A single amino acid substitution can shift the optimum pH of DNase I for enzyme activity: Biochemical and molecular analysis of the piscine DNase I family

Author keywords

cDNA cloning; Deoxyribonuclease I; Fish; Molecular evolution; Optimum pH; Purification

Indexed keywords

AMINO ACID; ASPARTIC ACID; COMPLEMENTARY DNA; DEOXYRIBONUCLEASE I; ENZYME; HISTIDINE;

EID: 2942538267     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2004.03.012     Document Type: Article
Times cited : (16)

References (45)
  • 1
    • 77956944804 scopus 로고
    • Pancreatic DNase
    • Boyer P.D. 3rd ed. New York: Academic Press
    • Moore S. Pancreatic DNase. Boyer P.D. 3rd ed. The Enzymes. vol. 14:1981;281-296 Academic Press, New York
    • (1981) The Enzymes , vol.14 , pp. 281-296
    • Moore, S.1
  • 2
    • 0027414010 scopus 로고
    • Measurement of deoxyribonuclease I activity in human tissues and body fluids by a single radial enzyme-diffusion method
    • Nadano D., Yasuda T., Kishi K. Measurement of deoxyribonuclease I activity in human tissues and body fluids by a single radial enzyme-diffusion method. Clin. Chem. 39:1993;448-452
    • (1993) Clin. Chem. , vol.39 , pp. 448-452
    • Nadano, D.1    Yasuda, T.2    Kishi, K.3
  • 3
    • 0034673555 scopus 로고    scopus 로고
    • Mammalian deoxyribonucleases I are classified into three types: Pancreas, parotid, and pancreas-parotid (mixed), based on differences in their tissue concentrations
    • Takeshita H., Mogi K., Yasuda T., Nakajima T., Nakashima Y., Mori S., Hoshino T., Kishi K. Mammalian deoxyribonucleases I are classified into three types: pancreas, parotid, and pancreas-parotid (mixed), based on differences in their tissue concentrations. Biochem. Biophys. Res. Commun. 269:2000;481-484
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 481-484
    • Takeshita, H.1    Mogi, K.2    Yasuda, T.3    Nakajima, T.4    Nakashima, Y.5    Mori, S.6    Hoshino, T.7    Kishi, K.8
  • 5
    • 0028342410 scopus 로고
    • Distribution of deoxyribonuclease I in rat tissues and its correlation to cellular turnover and apoptosis (programmed cell death)
    • Polzar B., Zanotti S., Stephan H., Rauch F., Peitsch M.C., Irmler M., Tschopp J., Mannherz H.G. Distribution of deoxyribonuclease I in rat tissues and its correlation to cellular turnover and apoptosis (programmed cell death). Eur. J. Cell Biol. 64:1994;200-210
    • (1994) Eur. J. Cell Biol. , vol.64 , pp. 200-210
    • Polzar, B.1    Zanotti, S.2    Stephan, H.3    Rauch, F.4    Peitsch, M.C.5    Irmler, M.6    Tschopp, J.7    Mannherz, H.G.8
  • 8
    • 0025336876 scopus 로고
    • Human serum deoxyribonuclease I (DNase I) polymorphism: Pattern similarities among isozymes from serum, urine, kidney, liver and pancreas
    • Kishi K., Yasuda T., Ikehara Y., Sawazaki K., Sato W., Iida R. Human serum deoxyribonuclease I (DNase I) polymorphism: pattern similarities among isozymes from serum, urine, kidney, liver and pancreas. Am. J. Hum. Genet. 47:1990;121-126
    • (1990) Am. J. Hum. Genet. , vol.47 , pp. 121-126
    • Kishi, K.1    Yasuda, T.2    Ikehara, Y.3    Sawazaki, K.4    Sato, W.5    Iida, R.6
  • 9
    • 0033600192 scopus 로고    scopus 로고
    • A new allele, DNASE1*6, oh human deoxyribonuclease I polymorphism encodes an Arg to Cys substitution responsible for its stability
    • Yasuda T., Takeshita H., Iida R., Kogure K., Kishi K. A new allele, DNASE1*6, oh human deoxyribonuclease I polymorphism encodes an Arg to Cys substitution responsible for its stability. Biochem. Biophys. Res. Commun. 260:1999;280-283
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 280-283
    • Yasuda, T.1    Takeshita, H.2    Iida, R.3    Kogure, K.4    Kishi, K.5
  • 10
    • 0032080726 scopus 로고    scopus 로고
    • Phenotype 2 of deoxyribonuclease I may be used as a risk factor for gastric carcinoma
    • Tsutsumi S., Asao T., Nagamachi Y., Nakajima T., Yasuda T., Kishi K. Phenotype 2 of deoxyribonuclease I may be used as a risk factor for gastric carcinoma. Cancer. 82:1998;1621-1625
    • (1998) Cancer , vol.82 , pp. 1621-1625
    • Tsutsumi, S.1    Asao, T.2    Nagamachi, Y.3    Nakajima, T.4    Yasuda, T.5    Kishi, K.6
  • 13
    • 0019797317 scopus 로고
    • Serum deoxyribonuclease I and clinical activity in systemic lupus erythematosus
    • Chitrabamrung S., Rubin R.L., Tan E.M. Serum deoxyribonuclease I and clinical activity in systemic lupus erythematosus. Rheumatol. Int. 1:1981;55-60
    • (1981) Rheumatol. Int. , vol.1 , pp. 55-60
    • Chitrabamrung, S.1    Rubin, R.L.2    Tan, E.M.3
  • 14
    • 0024997069 scopus 로고
    • Human genetically polymorphic deoxyribonuclease: Purification, characterization, and multiplicity of urine deoxyribonuclease I
    • Yasuda T., Awazu S., Sato W., Iida R., Tanaka Y., Kishi K. Human genetically polymorphic deoxyribonuclease: purification, characterization, and multiplicity of urine deoxyribonuclease I. J. Biochem. 108:1990;393-398
    • (1990) J. Biochem. , vol.108 , pp. 393-398
    • Yasuda, T.1    Awazu, S.2    Sato, W.3    Iida, R.4    Tanaka, Y.5    Kishi, K.6
  • 15
    • 0028799098 scopus 로고
    • Deoxyribonuclease I from rat urine: Affinity purification, characterization, and immunochemical studies
    • Takeshita H., Yasuda T., Nadano D., Iida R., Kishi K. Deoxyribonuclease I from rat urine: affinity purification, characterization, and immunochemical studies. J. Biochem. 118:1995;932-938
    • (1995) J. Biochem. , vol.118 , pp. 932-938
    • Takeshita, H.1    Yasuda, T.2    Nadano, D.3    Iida, R.4    Kishi, K.5
  • 16
    • 0030753025 scopus 로고    scopus 로고
    • Rabbit DNase I: Purification from urine, immunological and proteochemical characterization, nucleotide sequence, expression in tissues, relationships with other mammalian DNases I and phylogenetic analysis
    • Yasuda T., Takeshita H., Nakajima T., Hosomi O., Nakashima Y., Kishi K. Rabbit DNase I: purification from urine, immunological and proteochemical characterization, nucleotide sequence, expression in tissues, relationships with other mammalian DNases I and phylogenetic analysis. Biochem. J. 325:1997;465-473
    • (1997) Biochem. J. , vol.325 , pp. 465-473
    • Yasuda, T.1    Takeshita, H.2    Nakajima, T.3    Hosomi, O.4    Nakashima, Y.5    Kishi, K.6
  • 17
    • 0031410738 scopus 로고    scopus 로고
    • Mouse deoxyribonuclease I (DNase I): Biochemical and immunological characterizations, cDNA structure and tissue distribution
    • Takeshita H., Yasuda T., Nakajima T., Hosomi O., Nakashima Y., Kishi K. Mouse deoxyribonuclease I (DNase I): biochemical and immunological characterizations, cDNA structure and tissue distribution. Biochem. Mol. Biol. Int. 42:1997;65-75
    • (1997) Biochem. Mol. Biol. Int. , vol.42 , pp. 65-75
    • Takeshita, H.1    Yasuda, T.2    Nakajima, T.3    Hosomi, O.4    Nakashima, Y.5    Kishi, K.6
  • 20
    • 0037238047 scopus 로고    scopus 로고
    • A single amino acid substitution of Leu130Ile in snake DNases I contributes to the acquisition of thermal stability: A clue to the molecular evolutionary mechanism from cold-blooded to warm-blooded vertebrates
    • Takeshita H., Yasuda T., Nakajima T., Mogi K., Kaneko Y., Iida R., Kishi K. A single amino acid substitution of Leu130Ile in snake DNases I contributes to the acquisition of thermal stability: A clue to the molecular evolutionary mechanism from cold-blooded to warm-blooded vertebrates. Eur. J. Biochem. 270:2003;307-314
    • (2003) Eur. J. Biochem. , vol.270 , pp. 307-314
    • Takeshita, H.1    Yasuda, T.2    Nakajima, T.3    Mogi, K.4    Kaneko, Y.5    Iida, R.6    Kishi, K.7
  • 23
    • 0030662716 scopus 로고    scopus 로고
    • Purification and characterization of tilapia (Oreochromis mossambicus) deoxyribonuclease I - Primary structure and cDNA sequence
    • Hsiao Y.-M., Ho H.-C., Wang W.-T., Tam M.F., Liao T.-H. Purification and characterization of tilapia (Oreochromis mossambicus) deoxyribonuclease I - primary structure and cDNA sequence. Eur. J. Biochem. 249:1997;786-791
    • (1997) Eur. J. Biochem. , vol.249 , pp. 786-791
    • Hsiao, Y.-M.1    Ho, H.-C.2    Wang, W.-T.3    Tam, M.F.4    Liao, T.-H.5
  • 25
    • 0032517955 scopus 로고    scopus 로고
    • Activity measurement for deoxyribonucleases I and II with picogram sensitivity based on DNA/SYBR Green I fluorescence
    • Yasuda T., Takeshita H., Nakazato E., Nakajima T., Hosomi O., Nakashima Y., Kishi K. Activity measurement for deoxyribonucleases I and II with picogram sensitivity based on DNA/SYBR Green I fluorescence. Anal. Biochem. 255:1998;274-276
    • (1998) Anal. Biochem. , vol.255 , pp. 274-276
    • Yasuda, T.1    Takeshita, H.2    Nakazato, E.3    Nakajima, T.4    Hosomi, O.5    Nakashima, Y.6    Kishi, K.7
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.). 227:1970;680-685
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0031862990 scopus 로고    scopus 로고
    • Two novel screening methods for selecting monoclonal antibodies which specifically inhibit DNase I enzyme activity
    • Nakajima T., Yasuda T., Nakashima Y., Hosomi O., Takeshita H., Kishi K. Two novel screening methods for selecting monoclonal antibodies which specifically inhibit DNase I enzyme activity. Immunol. Invest. 27:1998;145-152
    • (1998) Immunol. Invest. , vol.27 , pp. 145-152
    • Nakajima, T.1    Yasuda, T.2    Nakashima, Y.3    Hosomi, O.4    Takeshita, H.5    Kishi, K.6
  • 28
    • 0000914609 scopus 로고    scopus 로고
    • 3rd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Sambrook J., Russell D.W. 3rd ed. Molecular Cloning: A Laboratory Manual. vol. 3:2001;17.1-17.112 Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • (2001) Molecular Cloning: A Laboratory Manual , vol.3 , pp. 171-17112
    • Sambrook, J.1    Russell, D.W.2
  • 29
    • 0028917808 scopus 로고
    • Structure of the human deoxyribonuclease I (DNase I) gene: Identification of the nucleotide substitution that generates its classical genetic polymorphism
    • Yasuda T., Kishi K., Yanagawa Y., Yoshida A. Structure of the human deoxyribonuclease I (DNase I) gene: identification of the nucleotide substitution that generates its classical genetic polymorphism. Ann. Hum. Genet. 59:1995;1-15
    • (1995) Ann. Hum. Genet. , vol.59 , pp. 1-15
    • Yasuda, T.1    Kishi, K.2    Yanagawa, Y.3    Yoshida, A.4
  • 30
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho S.N., Hunt H.D., Horton R.M., Pullen J.K., Pease L.R. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:1989;51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 31
    • 0033599572 scopus 로고    scopus 로고
    • Structural requirement of a human deoxyribonuclease II for the development of the active enzyme form, revealed by site-directed mutagenesis
    • Yasuda T., Takeshita H., Iida R., Nakajima T., Hosomi O., Nakashima Y., Mori S., Kishi K. Structural requirement of a human deoxyribonuclease II for the development of the active enzyme form, revealed by site-directed mutagenesis. Biochem. Biophys. Res. Commun. 256:1999;591-594
    • (1999) Biochem. Biophys. Res. Commun. , vol.256 , pp. 591-594
    • Yasuda, T.1    Takeshita, H.2    Iida, R.3    Nakajima, T.4    Hosomi, O.5    Nakashima, Y.6    Mori, S.7    Kishi, K.8
  • 33
    • 0025663466 scopus 로고
    • Nucleotide sequence of a full length cDNA clone encoding the deoxyribonuclease I from the rat parotid gland
    • Polzar B., Mannherz H.G. Nucleotide sequence of a full length cDNA clone encoding the deoxyribonuclease I from the rat parotid gland. Nucleic Acids Res. 18:1990;7151
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7151
    • Polzar, B.1    Mannherz, H.G.2
  • 34
    • 0032509815 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of a cDNA encoding bovine pancreatic deoxyribonuclease I in Escherichia coli: Purification and characterization of the recombinant enzyme
    • Chen C.-Y., Lu S.-C., Liao T.-H. Cloning, sequencing and expression of a cDNA encoding bovine pancreatic deoxyribonuclease I in Escherichia coli: purification and characterization of the recombinant enzyme. Gene. 206:1998;181-184
    • (1998) Gene , vol.206 , pp. 181-184
    • Chen, C.-Y.1    Lu, S.-C.2    Liao, T.-H.3
  • 35
    • 0022993944 scopus 로고
    • Comparison of the three primary structures of deoxyribonuclease isolated from bovine, ovine, and porcine pancreas. Derivation of the amino acid sequence of ovine DNase and revision of the previously published amino acid sequence of bovine DNase
    • Paudel H.K., Liao T.-H. Comparison of the three primary structures of deoxyribonuclease isolated from bovine, ovine, and porcine pancreas. Derivation of the amino acid sequence of ovine DNase and revision of the previously published amino acid sequence of bovine DNase. J. Biol. Chem. 261:1986;16012-16017
    • (1986) J. Biol. Chem. , vol.261 , pp. 16012-16017
    • Paudel, H.K.1    Liao, T.-H.2
  • 36
    • 17044447168 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the catalytic residues of bovine pancreatic deoxyribonuclease I
    • Jones S.J., Worrall A.F., Connolly B.A. Site-directed mutagenesis of the catalytic residues of bovine pancreatic deoxyribonuclease I. J. Mol. Biol. 264:1996;1154-1163
    • (1996) J. Mol. Biol. , vol.264 , pp. 1154-1163
    • Jones, S.J.1    Worrall, A.F.2    Connolly, B.A.3
  • 37
    • 0023038391 scopus 로고
    • Crystallographic refinement and structure of DNase I at 2 Å resolution
    • Oefner C., Suck D. Crystallographic refinement and structure of DNase I at 2 Å resolution. J. Mol. Biol. 192:1986;605-632
    • (1986) J. Mol. Biol. , vol.192 , pp. 605-632
    • Oefner, C.1    Suck, D.2
  • 38
    • 0031935579 scopus 로고    scopus 로고
    • Mutational analysis of human DNase I at the DNA binding interface: Implications for DNA recognition, catalysis, and metal ion dependence
    • Pan C.Q., Ulmer J.S., Herzka A., Lazarus R.A. Mutational analysis of human DNase I at the DNA binding interface: implications for DNA recognition, catalysis, and metal ion dependence. Protein Sci. 7:1998;628-636
    • (1998) Protein Sci. , vol.7 , pp. 628-636
    • Pan, C.Q.1    Ulmer, J.S.2    Herzka, A.3    Lazarus, R.A.4
  • 39
    • 0021511076 scopus 로고
    • Three-dimensional structure of bovine pancreatic DNase I at 2.5 Å resolution
    • Suck D., Oefner C., Kabsch W. Three-dimensional structure of bovine pancreatic DNase I at 2.5 Å resolution. EMBO J. 3:1984;2423-2430
    • (1984) EMBO J. , vol.3 , pp. 2423-2430
    • Suck, D.1    Oefner, C.2    Kabsch, W.3
  • 40
    • 0026354983 scopus 로고
    • DNase I-induced DNA conformation: 2 Å structure of a DNase I-octamer complex
    • Lahm A., Suck D. DNase I-induced DNA conformation: 2 Å structure of a DNase I-octamer complex. J. Mol. Biol. 221:1991;645-667
    • (1991) J. Mol. Biol. , vol.221 , pp. 645-667
    • Lahm, A.1    Suck, D.2
  • 42
    • 0032496170 scopus 로고    scopus 로고
    • Hyperreactivity of human DNase I variants: Dependence on the number of positively charged residues and concentration, length, and environment of DNA
    • Pan C.Q., Lazarus R.A. Hyperreactivity of human DNase I variants: dependence on the number of positively charged residues and concentration, length, and environment of DNA. J. Biol. Chem. 273:1998;11701-11708
    • (1998) J. Biol. Chem. , vol.273 , pp. 11701-11708
    • Pan, C.Q.1    Lazarus, R.A.2
  • 43
    • 0030966960 scopus 로고    scopus 로고
    • Engineering hyperactive variants of human deoxyribonuclease I by altering its functional mechanism
    • Pan C.Q., Lazarus R.A. Engineering hyperactive variants of human deoxyribonuclease I by altering its functional mechanism. Biochemistry. 36:1997;6624-6632
    • (1997) Biochemistry , vol.36 , pp. 6624-6632
    • Pan, C.Q.1    Lazarus, R.A.2
  • 44
    • 0018068264 scopus 로고
    • Gas exchange in the carp gills in normoxic and hypoxic conditions
    • Itazawa Y., Takeda T. Gas exchange in the carp gills in normoxic and hypoxic conditions. Respir. Physiol. 35:1978;263-269
    • (1978) Respir. Physiol. , vol.35 , pp. 263-269
    • Itazawa, Y.1    Takeda, T.2
  • 45
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou N., Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4:1987;406-425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.