Function of the loop residue Thr792 in human DNA topoisomerase IIα

Namiko Suda, Yoshiyuki Nakagawa, Akihiko Kikuchi, Masako Sawada, Yuko Takami, Hiro Omi Funahashi, Akimasa Nakao, Shonen Yoshida, Motoshi Suzuki

研究成果: Article

3 引用 (Scopus)

抄録

We studied the mutation effect of one of the putative loop residues Thr792 in human DNA topoisomerase IIα (TOP2α). Thr792 mutants were expressed from high or low copy plasmids in a temperature sensitive yeast strain deficient in TOP2 (top2-1). When expressed from a high copy plasmid, mutants with small side chains complemented the yeast defect; however, from a low copy plasmid, only wild-type, Ser, and Cys substitution mutants complemented the yeast defect. Interestingly, at the permissive temperature other mutants (e.g., Val, Gly, and Glu substitutions) showed the dominant negative effect to the top2-1 allele, which was not observed by the control α4-helix mutants. T792E mutant was 10-fold less active than wild-type and the T792P had no decatenation activity in vitro. These results suggest that Thr792 in human TOP2α is involved in enzyme catalysis.

元の言語English
ページ(範囲)46-51
ページ数6
ジャーナルBiochemical and Biophysical Research Communications
303
発行部数1
DOI
出版物ステータスPublished - 28-03-2003
外部発表Yes

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Type II DNA Topoisomerase
Yeast
Plasmids
Yeasts
Substitution reactions
Defects
Temperature
Catalysis
Alleles
Mutation
Enzymes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

これを引用

Suda, Namiko ; Nakagawa, Yoshiyuki ; Kikuchi, Akihiko ; Sawada, Masako ; Takami, Yuko ; Funahashi, Hiro Omi ; Nakao, Akimasa ; Yoshida, Shonen ; Suzuki, Motoshi. / Function of the loop residue Thr792 in human DNA topoisomerase IIα. :: Biochemical and Biophysical Research Communications. 2003 ; 巻 303, 番号 1. pp. 46-51.
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abstract = "We studied the mutation effect of one of the putative loop residues Thr792 in human DNA topoisomerase IIα (TOP2α). Thr792 mutants were expressed from high or low copy plasmids in a temperature sensitive yeast strain deficient in TOP2 (top2-1). When expressed from a high copy plasmid, mutants with small side chains complemented the yeast defect; however, from a low copy plasmid, only wild-type, Ser, and Cys substitution mutants complemented the yeast defect. Interestingly, at the permissive temperature other mutants (e.g., Val, Gly, and Glu substitutions) showed the dominant negative effect to the top2-1 allele, which was not observed by the control α4-helix mutants. T792E mutant was 10-fold less active than wild-type and the T792P had no decatenation activity in vitro. These results suggest that Thr792 in human TOP2α is involved in enzyme catalysis.",
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Suda, N, Nakagawa, Y, Kikuchi, A, Sawada, M, Takami, Y, Funahashi, HO, Nakao, A, Yoshida, S & Suzuki, M 2003, 'Function of the loop residue Thr792 in human DNA topoisomerase IIα', Biochemical and Biophysical Research Communications, 巻. 303, 番号 1, pp. 46-51. https://doi.org/10.1016/S0006-291X(03)00297-3

Function of the loop residue Thr792 in human DNA topoisomerase IIα. / Suda, Namiko; Nakagawa, Yoshiyuki; Kikuchi, Akihiko; Sawada, Masako; Takami, Yuko; Funahashi, Hiro Omi; Nakao, Akimasa; Yoshida, Shonen; Suzuki, Motoshi.

:: Biochemical and Biophysical Research Communications, 巻 303, 番号 1, 28.03.2003, p. 46-51.

研究成果: Article

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T1 - Function of the loop residue Thr792 in human DNA topoisomerase IIα

AU - Suda, Namiko

AU - Nakagawa, Yoshiyuki

AU - Kikuchi, Akihiko

AU - Sawada, Masako

AU - Takami, Yuko

AU - Funahashi, Hiro Omi

AU - Nakao, Akimasa

AU - Yoshida, Shonen

AU - Suzuki, Motoshi

PY - 2003/3/28

Y1 - 2003/3/28

N2 - We studied the mutation effect of one of the putative loop residues Thr792 in human DNA topoisomerase IIα (TOP2α). Thr792 mutants were expressed from high or low copy plasmids in a temperature sensitive yeast strain deficient in TOP2 (top2-1). When expressed from a high copy plasmid, mutants with small side chains complemented the yeast defect; however, from a low copy plasmid, only wild-type, Ser, and Cys substitution mutants complemented the yeast defect. Interestingly, at the permissive temperature other mutants (e.g., Val, Gly, and Glu substitutions) showed the dominant negative effect to the top2-1 allele, which was not observed by the control α4-helix mutants. T792E mutant was 10-fold less active than wild-type and the T792P had no decatenation activity in vitro. These results suggest that Thr792 in human TOP2α is involved in enzyme catalysis.

AB - We studied the mutation effect of one of the putative loop residues Thr792 in human DNA topoisomerase IIα (TOP2α). Thr792 mutants were expressed from high or low copy plasmids in a temperature sensitive yeast strain deficient in TOP2 (top2-1). When expressed from a high copy plasmid, mutants with small side chains complemented the yeast defect; however, from a low copy plasmid, only wild-type, Ser, and Cys substitution mutants complemented the yeast defect. Interestingly, at the permissive temperature other mutants (e.g., Val, Gly, and Glu substitutions) showed the dominant negative effect to the top2-1 allele, which was not observed by the control α4-helix mutants. T792E mutant was 10-fold less active than wild-type and the T792P had no decatenation activity in vitro. These results suggest that Thr792 in human TOP2α is involved in enzyme catalysis.

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