Reversible binding of zinc in Plasmodium falciparum Sir2: Structure and activity of the apoenzyme

被引：23

作者：

Chakrabarty, Subhra Prakash ^{[1
]}

Balaram, Hemalatha ^{[1
]}

机构：

[1] Jawaharlal Nehru Ctr Adv Sci Res, Mol Biol & Genet Unit, Bangalore 560064, Karnataka, India

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2010年 / 1804卷 / 09期

关键词：

Sir2; Plasmodium falciparum; Zinc affinity; Deacetylase activity; Structural stability; Zinc reconstitution; COLI ASPARTATE TRANSCARBAMOYLASE; ESCHERICHIA-COLI; NAD(+)-DEPENDENT DEACETYLASE; VIRULENCE GENES; PROTEIN; METAL; AFFINITY; RELEASE; FINGER; FAMILY;

D O I：

10.1016/j.bbapap.2010.06.010

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2010 Elsevier B.V. All rights reserved.

引用

页码：1743 / 1750

页数：8

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