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Titolo:
Purification and characterization of a novel DNA repair enzyme from the extremely radioresistant bacterium Rubrobacter radiotolerans
Autore:
Asgarani, E; Terato, H; Asagoshi, K; Shahmohammadi, HR; Ohyama, Y; Saito, T; Yamamoto, O; Ide, H;
Indirizzi:
Hiroshima Univ, Grad Sch Sci, Dept Math & Life Sci, Higashihiroshima 7398526, Japan Hiroshima Univ Higashihiroshima Japan 7398526 hihiroshima 7398526, Japan Hiroshima Univ, Radioisotope Ctr, Higashihiroshima 7398526, Japan Hiroshima Univ Higashihiroshima Japan 7398526 hihiroshima 7398526, Japan Hiroshima Int Univ, Fac Hlth Sci, Dept Clin Radiol, Hiroshima 7240695, Japan Hiroshima Int Univ Hiroshima Japan 7240695 iol, Hiroshima 7240695, Japan
Titolo Testata:
JOURNAL OF RADIATION RESEARCH
fascicolo: 1, volume: 41, anno: 2000,
pagine: 19 - 34
SICI:
0449-3060(200003)41:1<19:PACOAN>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
COLI ENDONUCLEASE-III; DEINOCOCCUS-RADIODURANS; ESCHERICHIA-COLI; HALOBACTERIUM-SALINARIUM; UREA RESIDUES; DAMAGE; GENE; BACTERIORUBERIN; IDENTIFICATION; GLYCOSYLASE;
Keywords:
radioresistant bacteria; repair enzyme; thymine glycol; enzyme purification; endonuclease III; homologue;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Ide, H Hiroshima Univ, Grad Sch Sci, Dept Math & Life Sci, Higashihiroshima 7398526, Japan Hiroshima Univ Higashihiroshima Japan 7398526 hima 7398526, Japan
Citazione:
E. Asgarani et al., "Purification and characterization of a novel DNA repair enzyme from the extremely radioresistant bacterium Rubrobacter radiotolerans", J RADIAT R, 41(1), 2000, pp. 19-34

Abstract

Rubrobacter radiotolerans is an extremely radioresistant bacterium. It exhibits higher resistance than the well-known radioresistant bacterium Deinococcus radiodurans, but the molecular mechanisms responsible for the radioresistance of R. radiotolerans remain unknown. In the present study, we have demonstrated the presence of a novel DNA repair enzyme in R. radiotolerans cells that recognizes radiation-induced DNA damages such as thymine glycol,urea residues, and abasic sites. The enzyme was purified from the crude cell extract by a series of chromatography to an apparent physical homogeneity. The purified enzyme showed a single band with a molecular mass of approximately 40 kDa in SDS-polyacrylamide gel electrophoresis, and was designated as R-endonuclease. R-Endonuclease exhibited repair activity for thymine glycol, urea residues, and abasic sites present in plasmid DNA, but did not act on intact DNA, UV-irradiated DNA and DNA containing reduced abasic sites. The substrate specificity together with the salt and pH optima suggests that R-endonuclease is a functional homolog of endonuclease III of Escherichia coli.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/09/20 alle ore 13:30:52