作者: N. Padmaja , Hema Rajaram , Shree Kumar Apte
DOI: 10.1016/J.ABB.2010.10.007
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摘要: Abstract The open reading frame alr3199 of the nitrogen-fixing cyanobacterium, Anabaena sp. strain PCC7120 was cloned and overexpressed in Escherichia coli . Purified recombinant Alr3199 protein found to be a functionally active deoxyribonuclease with novel features, such as (1) no homology typical DNases (2) Ca 2+ -dependent Nickase activity (3) presence di-hemerythrin domain, (4) requirement Fe conjugated hemerythrin domains for optimal activity. Both DNase activities were associated N-terminal non-hemerythrin region, but modulated by C-terminal region. This is first report activity, tentatively designated ‘HE-DNase’, possible role stress-induced DNA damage/repair