Sequence specific interaction of Mycobacterium smegmatis topoisomerase I with duplex DNA


Autoria(s): Bhaduri, T; Sikder, D; Nagaraja, V
Data(s)

01/04/1998

Resumo

We have identified strong topoisomerase sites (STS) for Mycobacteruim smegmatis topoisomerase I in double-stranded DNA context using electrophoretic mobility shift assay of enzyme-DNA covalent complexes; Mg2+, an essential component for DNA relaxation activity of the enzyme, is not required for binding to DNA, The enzyme makes single-stranded nicks, with transient covalent interaction at the 5'-end of the broken DNA strand, a characteristic akin to prokaryotic topoisomerases. More importantly, the enzyme binds to duplex DNA having a preferred site with high affinity, a. property similar to the eukaryotic type I topoisomerases, The preferred cleavage site is mapped on a 65 bp duplex DNA and found to be CG/TCTT. Thus, the enzyme resembles other prokaryotic type I topoisomerases in mechanistics of the reaction, but is similar to eukaryotic enzymes in DNA recognition properties.

Formato

application/pdf

Identificador

http://eprints.iisc.ernet.in/19225/1/Sequence_specific_interaction.pdf

Bhaduri, T and Sikder, D and Nagaraja, V (1998) Sequence specific interaction of Mycobacterium smegmatis topoisomerase I with duplex DNA. In: Nucleic Acids Research, 26 (07). pp. 1668-1674.

Publicador

Oxford University Press

Relação

http://nar.oxfordjournals.org/cgi/content/abstract/26/7/1668

http://eprints.iisc.ernet.in/19225/

Palavras-Chave #Microbiology & Cell Biology
Tipo

Journal Article

PeerReviewed