ATP-INDEPENDENT DNA TOPOISOMERASE FROM FERVIDOBACTERIUM-ISLANDICUM

DELATOUR, CB and PORTEMER, C and FORTERRE, P and HUBER, R and DUGUET, M (1993) ATP-INDEPENDENT DNA TOPOISOMERASE FROM FERVIDOBACTERIUM-ISLANDICUM. BIOCHIMICA ET BIOPHYSICA ACTA, 1216 (2). pp. 213-220. ISSN 0006-3002,

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Abstract

Thermotogales are thermophilic eubacteria belonging to a very slowly evolving branch in the eubacterial tree. In this report, we describe the purification and characterization of an ATP-independent DNA topoisomerase from the Thermotogale, Fervidobacterium islandicum. The enzyme, a monomer of about 75 kDa, is a type I DNA topoisomerase sharing many properties with the other bacterial topoisomerases I: it absolutely requires Mg2+ for activity, relaxes negatively but not positively supercoiled DNA and is inhibited by single-stranded M13 DNA and spermidine. A feature of the F. islandicum ATP-independent DNA topoisomerase I is its thermophily. The optimal temperature for the enzymatic activity is 75-degrees-C. Studies about thermostability show that the enzyme is more stable when incubated undiluted in the storage buffer. In these conditions, 60% activity was retained after a 30 min preincubation at 75-degrees-C.

Item Type: Article
Uncontrolled Keywords: ESCHERICHIA-COLI; REVERSE GYRASE; DESULFUROCOCCUS-AMYLOLYTICUS; OMEGA-PROTEIN; ARCHAEBACTERIA; PURIFICATION; IDENTIFICATION; SEQUENCE; INVITRO; ENZYME; DNA TOPOISOMERASE-I; BACTERIUM; THERMOTOGA; THERMOPHILE; (F-ISLANDICUM)
Depositing User: Dr. Gernot Deinzer
Last Modified: 19 Oct 2022 08:42
URI: https://pred.uni-regensburg.de/id/eprint/53671

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