A novel hemerythrin DNase from the nitrogen-fixing cyanobacterium Anabaena sp. strain PCC7120
► Alr3199 is functionally active as a DNase or Nickase depending on nature and concentration of cation present. ► Alr3199 has no domain homology with DNase/nicking endonuclease, but has two hemerythrin domains in the C-terminus. ► DNase/Nickase activity of Alr3199 resides in the N-terminal non-hemer...
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Veröffentlicht in: | Archives of biochemistry and biophysics 2011-01, Vol.505 (2), p.171-177 |
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Sprache: | eng |
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Zusammenfassung: | ► Alr3199 is functionally active as a DNase or Nickase depending on nature and concentration of cation present. ► Alr3199 has no domain homology with DNase/nicking endonuclease, but has two hemerythrin domains in the C-terminus. ► DNase/Nickase activity of Alr3199 resides in the N-terminal non-hemerythrin region and is modulated by Fe2+ bound to the C-terminal hemerythrin region. ► Alr3199 is the only hemerythrin protein known to have a DNase activity.
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 was found to be a functionally active deoxyribonuclease with novel features, such as (1) no homology to typical DNases (2) a Ca2+-dependent Nickase activity (3) presence of a di-hemerythrin domain, and (4) requirement of Fe2+ conjugated to hemerythrin domains for optimal activity. Both the DNase and Nickase activities were found to be associated with the N-terminal non-hemerythrin region, but were modulated by Fe2+ conjugated to the C-terminal hemerythrin region. This is the first report of a hemerythrin protein with DNase activity, tentatively designated as ‘HE-DNase’, and with a possible role in stress-induced DNA damage/repair in Anabaena. |
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ISSN: | 0003-9861 1096-0384 |
DOI: | 10.1016/j.abb.2010.10.007 |