메뉴 건너뛰기




Volumn 199, Issue 1-2, 1997, Pages 77-82

Cloning and characterization of the uvrD gene from an extremely thermophilic bacterium, Thermus thermophilus HB8

Author keywords

Complementation; DNA helicase; DNA repair; Nucleotide excision repair; UV sensitivity

Indexed keywords

ASPARAGINE; CYSTEINE; GLUTAMINE; HELICASE; METHIONINE; PROLINE;

EID: 0030866053     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(97)00349-1     Document Type: Article
Times cited : (10)

References (28)
  • 2
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • Doig, A.J., Williams, D.H., 1991. Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J. Mol. Biol. 217, 389-398.
    • (1991) J. Mol. Biol. , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 5
    • 0027491528 scopus 로고
    • Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution
    • Fujinaga, M., Berthet-Colominas, C., Yaremchuk, A.D., Tukalo, M. A., Cusack, S., 1993. Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution. J. Mol. Biol. 234, 222-233.
    • (1993) J. Mol. Biol. , vol.234 , pp. 222-233
    • Fujinaga, M.1    Berthet-Colominas, C.2    Yaremchuk, A.D.3    Tukalo, M.A.4    Cusack, S.5
  • 6
    • 0023089713 scopus 로고
    • Escherichia coli rep gene: Sequence of the gene, the encoded helicase, and its homology with uvrD
    • Gilchrist, C.A., Denhardt, D.T., 1987. Escherichia coli rep gene: sequence of the gene, the encoded helicase, and its homology with uvrD. Nucleic Acids Res. 15, 465-475.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 465-475
    • Gilchrist, C.A.1    Denhardt, D.T.2
  • 7
    • 0024344173 scopus 로고
    • Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes
    • Gorbalenya, A.E., Koonin, E.V., Donchenko, A.P., Blinov, V.M., 1989. Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. Nucleic Acids Res. 17, 4713-4730.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4713-4730
    • Gorbalenya, A.E.1    Koonin, E.V.2    Donchenko, A.P.3    Blinov, V.M.4
  • 8
    • 0021253525 scopus 로고
    • Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing
    • Henikoff, S., 1984. Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing. Gene 28, 351-359.
    • (1984) Gene , vol.28 , pp. 351-359
    • Henikoff, S.1
  • 9
    • 0026334204 scopus 로고
    • Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution
    • Imada, K., Sato, M., Tanaka, N., Katsube, Y., Matsuura, Y., Oshima, T., 1991. Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2 Å resolution. J. Mol. Biol. 222, 725-738.
    • (1991) J. Mol. Biol. , vol.222 , pp. 725-738
    • Imada, K.1    Sato, M.2    Tanaka, N.3    Katsube, Y.4    Matsuura, Y.5    Oshima, T.6
  • 10
    • 0027718002 scopus 로고
    • RecA protein from an extremely thermophilic bacterium, Thermus thermophilus HB8
    • Kato, R., Kuramitsu, S., 1993. RecA protein from an extremely thermophilic bacterium, Thermus thermophilus HB8. J. Biochem. 114, 926-929.
    • (1993) J. Biochem. , vol.114 , pp. 926-929
    • Kato, R.1    Kuramitsu, S.2
  • 11
    • 0029873181 scopus 로고    scopus 로고
    • ATPase activity of UvrB protein from Thermus thermophilus HB8 and its interaction with DNA
    • Kato, R., Yamamoto, N., Kito, K., Kuramitsu, S., 1996. ATPase activity of UvrB protein from Thermus thermophilus HB8 and its interaction with DNA. J. Biol. Chem. 271, 9612-9618.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9612-9618
    • Kato, R.1    Yamamoto, N.2    Kito, K.3    Kuramitsu, S.4
  • 12
    • 0029893874 scopus 로고    scopus 로고
    • Mechanism of helicase-catalyzed DNA unwinding
    • Lohman, T.M., Bjornson, K.M., 1996. Mechanism of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65, 169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.M.2
  • 13
    • 0029166296 scopus 로고
    • A multiple site-specific DNA-inversion model for the control of Omp1 phase and antigenic variation in Dichelobacter nodosus
    • Moses, E.K., Good, R.T., Sinistaj, M., Billington, S.J., Langford, C.J., Rood, J.I., 1995. A multiple site-specific DNA-inversion model for the control of Omp1 phase and antigenic variation in Dichelobacter nodosus. Mol. Microbiol. 17, 183-196.
    • (1995) Mol. Microbiol. , vol.17 , pp. 183-196
    • Moses, E.K.1    Good, R.T.2    Sinistaj, M.3    Billington, S.J.4    Langford, C.J.5    Rood, J.I.6
  • 15
    • 0014401726 scopus 로고
    • Studies on radiationsensitive mutants of E. coli. I. Mutants defective in the repair synthesis
    • Ogawa, H., Shimada, K., Tomizawa, J., 1968. Studies on radiationsensitive mutants of E. coli. I. Mutants defective in the repair synthesis. Mol. Gen. Genet. 101, 227-244.
    • (1968) Mol. Gen. Genet. , vol.101 , pp. 227-244
    • Ogawa, H.1    Shimada, K.2    Tomizawa, J.3
  • 16
    • 0030025487 scopus 로고    scopus 로고
    • An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8
    • Okamoto, A., Kato, R., Masui, R., Yamagishi, A., Oshima, T., Kuramitsu, S., 1996. An aspartate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. J. Biochem. 119, 135-144.
    • (1996) J. Biochem. , vol.119 , pp. 135-144
    • Okamoto, A.1    Kato, R.2    Masui, R.3    Yamagishi, A.4    Oshima, T.5    Kuramitsu, S.6
  • 17
    • 0015955554 scopus 로고
    • Description of Thermus thermophilus (Yoshida and Oshima) comb, nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa
    • Oshima, T., Imahori, K., 1974. Description of Thermus thermophilus (Yoshida and Oshima) comb, nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa. Int. J. Syst. Bacteriol. 24, 102-112.
    • (1974) Int. J. Syst. Bacteriol. , vol.24 , pp. 102-112
    • Oshima, T.1    Imahori, K.2
  • 22
    • 0001767586 scopus 로고
    • A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidase
    • Suzuki, Y., Oishi, K., Nakano, H., Nagayama, T., 1987. A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidase. Appl. Microbiol. Biotechnol. 26, 546-551.
    • (1987) Appl. Microbiol. Biotechnol. , vol.26 , pp. 546-551
    • Suzuki, Y.1    Oishi, K.2    Nakano, H.3    Nagayama, T.4
  • 23
    • 0030008073 scopus 로고    scopus 로고
    • Mismatch DNA recognition protein from an extremely thermophilic bacterium, Thermus thermophilus HB8
    • Takamatsu, S., Kato, R., Kuramitsu, S., 1996. Mismatch DNA recognition protein from an extremely thermophilic bacterium, Thermus thermophilus HB8. Nucleic Acids Res. 24, 640-648.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 640-648
    • Takamatsu, S.1    Kato, R.2    Kuramitsu, S.3
  • 24
    • 0027716997 scopus 로고
    • The sequence of the Haemophilus influenzae mutB gene indicates it encodes a DNA helicase II-like protein
    • Walter, R.B., Morton, K.A., Stuy, J.H., 1993. The sequence of the Haemophilus influenzae mutB gene indicates it encodes a DNA helicase II-like protein. Gene 136, 35-40.
    • (1993) Gene , vol.136 , pp. 35-40
    • Walter, R.B.1    Morton, K.A.2    Stuy, J.H.3
  • 25
    • 0026316725 scopus 로고
    • Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006
    • Watanabe, K., Chishiro, K., Kitamura, K., Suzuki, Y., 1991. Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-1,6-glucosidase from Bacillus thermoglucosidasius KP1006. J. Biol. Chem. 266, 24287-24294.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24287-24294
    • Watanabe, K.1    Chishiro, K.2    Kitamura, K.3    Suzuki, Y.4
  • 26
    • 0028130117 scopus 로고
    • Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule
    • Watanabe, K., Masuda, T., Ohashi, H., Mihara, H., Suzuki, Y., 1994. Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-1,6-glucosidase. Irrefragable proof supporting the proline rule. Eur. J. Biochem. 226, 277-283.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 277-283
    • Watanabe, K.1    Masuda, T.2    Ohashi, H.3    Mihara, H.4    Suzuki, Y.5
  • 27
    • 0029974683 scopus 로고    scopus 로고
    • Cloning, sequencing and expression of the uvrA gene from an extremely thermophilic bacterium, Thermus thermophilus HB8
    • Yamamoto, N., Kato, R., Kuramitsu, S., 1996. Cloning, sequencing and expression of the uvrA gene from an extremely thermophilic bacterium, Thermus thermophilus HB8. Gene 171, 103-106.
    • (1996) Gene , vol.171 , pp. 103-106
    • Yamamoto, N.1    Kato, R.2    Kuramitsu, S.3
  • 28
    • 0022728104 scopus 로고
    • Determination of the initiation sites of transcription and translation of the uvrD gene of Escherichia coli
    • Yamamoto, Y., Ogawa, T., Shinagawa, H., Nakayama, T., Matsuo, H., Ogawa, H., 1986. Determination of the initiation sites of transcription and translation of the uvrD gene of Escherichia coli. J. Biochem. 99, 1579-1590.
    • (1986) J. Biochem. , vol.99 , pp. 1579-1590
    • Yamamoto, Y.1    Ogawa, T.2    Shinagawa, H.3    Nakayama, T.4    Matsuo, H.5    Ogawa, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.