Literature DB >> 8002018

DNA topoisomerase I from Mycobacterium smegmatis.

T Bhaduri1, V Nagaraja.   

Abstract

DNA topoisomerase I has been purified from Mycobacterium smegmatis to near homogeneity using different column chromatographic techniques. The enzyme activity relaxes form I DNA into form IV DNA, requiring Mg2+, but not ATP or any other cofactors for its activity. Several properties of the enzyme were found to be similar to that of the prototype enzyme, Escherichia coli topoisomerase I.

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Year:  1994        PMID： 8002018

Source DB:  PubMed          Journal:  Indian J Biochem Biophys        ISSN： 0301-1208            Impact factor:   1.918


  3 in total

1.  Sequence specific interaction of Mycobacterium smegmatis topoisomerase I with duplex DNA.

Authors:  T Bhaduri; D Sikder; V Nagaraja
Journal:  Nucleic Acids Res       Date:  1998-04-01       Impact factor: 16.971

2.  Analysis of DNA relaxation and cleavage activities of recombinant Mycobacterium tuberculosis DNA topoisomerase I from a new expression and purification protocol.

Authors:  Thirunavukkarasu Annamalai; Neil Dani; Bokun Cheng; Yuk-Ching Tse-Dinh
Journal:  BMC Biochem       Date:  2009-06-11       Impact factor: 4.059

3.  A highly processive topoisomerase I: studies at the single-molecule level.

Authors:  Marcin Jan Szafran; Terence Strick; Agnieszka Strzałka; Jolanta Zakrzewska-Czerwińska; Dagmara Jakimowicz
Journal:  Nucleic Acids Res       Date:  2014-05-31       Impact factor: 16.971
  3 in total

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