Reversible binding of zinc in Plasmodium falciparum Sir2: Structure and activity of the apoenzyme |
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Authors: | Subhra Prakash Chakrabarty Hemalatha Balaram |
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Institution: | Molecular Biology and Genetics Unit, Jawaharlal Nehru Centre for Advanced Scientific Research, Jakkur, Bangalore 560064, India |
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Abstract: | Reversible zinc chelation via thiol groups of cysteines leading to modulation of activity in redox regulated proteins forms a basis for switching on–off of various biochemical processes. Silent information regulator 2 (Sir2), a NAD+ dependent deacetylase, contains a non-catalytic zinc ion coordinated by thiol groups of cysteines. Using Plasmodium falciparum Sir2 (PfSir2), we have examined the effect of zinc removal on the structure and activity of this enzyme. Our studies show that the enzyme with high affinity for zinc exhibits partial collapse of structure upon removal of the metal ion. Zinc reconstitution of apo PfSir2 led to recovery of both structure and activity highlighting the reversibility of the process. |
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Keywords: | Sir2 Plasmodium falciparum Zinc affinity Deacetylase activity Structural stability Zinc reconstitution |
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