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OPAC HELP

Titolo:
PURIFICATION OF 2 DNA-DEPENDENT ADENOSINE-TRIPHOSPHATASES HAVING DNA HELICASE ACTIVITY FROM HELA-CELLS AND COMPARISON OF THE PROPERTIES OF THE 2 ENZYMES
Autore:
SEKI M; YANAGISAWA J; KOHDA T; SONOYAMA T; UI M; ENOMOTO T;
Indirizzi:
UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM,BUNKYO KU,7-3-1 HONGOTOKYO 113 JAPAN UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM,BUNKYO KU TOKYO 113 JAPAN
Titolo Testata:
Journal of Biochemistry
fascicolo: 3, volume: 115, anno: 1994,
pagine: 523 - 531
SICI:
0021-924X(1994)115:3<523:PO2DAH>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
LARGE TUMOR-ANTIGEN; MOUSE FM3A CELLS; SACCHAROMYCES-CEREVISIAE; XERODERMA-PIGMENTOSUM; CALF THYMUS; ESCHERICHIA-COLI; REPAIR GENE; GROUP-C; PROTEIN; RAD3;
Keywords:
DNA-DEPENDENT ATPASE Q1; DNA-DEPENDENT ATPASE Q2; DNA HELICASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
M. Seki et al., "PURIFICATION OF 2 DNA-DEPENDENT ADENOSINE-TRIPHOSPHATASES HAVING DNA HELICASE ACTIVITY FROM HELA-CELLS AND COMPARISON OF THE PROPERTIES OF THE 2 ENZYMES", Journal of Biochemistry, 115(3), 1994, pp. 523-531

Abstract

DNA-dependent ATPase activities, in crude extracts prepared from HeLacells were separated into five peaks designated Q1 to Q5 by FPLC MonoQ column chromatography. In our previous study, we observed that crude extracts prepared from xeroderma pigmentosum complementation group C(XP-C) cells contained no DNA-dependent ATPase activity at the peak position of Q1 and exhibited a broader peak with higher activity than normal Q2 at the peak position of Q2 [Yanagisawa, J., Seki, M., Ui, M.,and Enomoto, T. (1992) J. Biol. Chem. 267, 3585-3588]. We have purified two DNA-dependent ATPases Q1 and Q2 from HeLa cells and characterized their properties in order to obtain a means to discriminate ATPase Q1 from Q2 in XP-C cells. The apparent molecular masses of Q1 and Q2 on SDS-polyacrylamide gel electrophoresis were 73 and 100 kDa, respectively. The two enzymes required a divalent cation for activity. DNA-dependent ATPase Q1 hydrolyzed ATP and dATP and Q2 hydrolyzed ATP preferentially among the nucleotides tested. Both enzymes preferred single-stranded DNA as a cofactor. The DNA-dependent ATPase activity of Q2 was inhibited by 90% in the presence of 200 mM NaCl, whereas that of Q1 was not affected by NaCl at concentrations up to 200 mM. Both enzymes had DNA helicase activity, that of Q1 being more resistant to NaCl than that of Q2. The DNA helicase activity of Q2 was about 150-fold higher than that of Q1, when compared with units of ATPase activity. The direction of unwinding for Q1 was from 3' to 5' and that for Q2 was 5' to 3' with respect to the DNA to which the enzymes bound. Examinations based on the differences in the properties of the two enzymes have indicated that DNA-dependent ATPase Q1 is altered in XP-C cells, resulting in the overlapping elution of Q1 and Q2.

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Documento generato il 01/10/20 alle ore 13:51:31