The structure of bradyzoite-specific enolase from Toxoplasma gondii reveals insights into its dual cytoplasmic and nuclear functions

Acta Crystallographica. Section D, Biological Crystallography
Jiapeng RuanHuân M Ngô

Abstract

In addition to catalyzing a central step in glycolysis, enolase assumes a remarkably diverse set of secondary functions in different organisms, including transcription regulation as documented for the oncogene c-Myc promoter-binding protein 1. The apicomplexan parasite Toxoplasma gondii differentially expresses two nuclear-localized, plant-like enolases: enolase 1 (TgENO1) in the latent bradyzoite cyst stage and enolase 2 (TgENO2) in the rapidly replicative tachyzoite stage. A 2.75 Å resolution crystal structure of bradyzoite enolase 1, the second structure to be reported of a bradyzoite-specific protein in Toxoplasma, captures an open conformational state and reveals that distinctive plant-like insertions are located on surface loops. The enolase 1 structure reveals that a unique residue, Glu164, in catalytic loop 2 may account for the lower activity of this cyst-stage isozyme. Recombinant TgENO1 specifically binds to a TTTTCT DNA motif present in the cyst matrix antigen 1 (TgMAG1) gene promoter as demonstrated by gel retardation. Furthermore, direct physical interactions of both nuclear TgENO1 and TgENO2 with the TgMAG1 gene promoter are demonstrated in vivo using chromatin immunoprecipitation (ChIP) assays. Structural and bi...Continue Reading

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Citations

Apr 27, 2017·Frontiers in Microbiology·Xiangye LiuKuiyang Zheng
Oct 23, 2018·Frontiers in Cellular and Infection Microbiology·Joseph D LykinsHuân M Ngô

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Methods Mentioned

BETA
gel filtration
X-ray
PISA
immunoprecipitation
ChIP
PCR

Software Mentioned

PyMOL
PISA
LigPlot +
Coot
3000
Phaser

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