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Calmodulin proximal interacting proteins revealed through BioID technology in the tachyzoite stage of Toxoplasma gondii

ABSTRACT: Toxoplasma gondii is an apicomplexan parasite infecting human and animals, causing huge health concerns and economic losses. Calcium ion, a critical second messenger in cells, can regulate related vital activities, particularly in parasite invasion and escape processes. Calmodulin (CaM) is a short, highly conserved Ca2+ binding protein found in all eukaryotic cells, including apicomplexan parasites. After binding to Ca2+, CaM can be activated to interact with a variety of proteins (such as enzymes). Nevertheless, CaM-interacting proteins have not been identified in T. gondii. We report here the use of T. gondii strain RH△hxgprt expressing the proximity-labeling enzyme BirA* fused to CaM, in combination with LC-MS/MS to specifically identify CaM-interacting proteins. Our study revealed over three hundred of CaM’s proximal interacting proteins in T. gondii. These CaM partners were broadly dispersed throughout the parasite. The majority of their CRISPR fitness scores were below zero, indicating CaM's essential functions in parasites.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Toxoplasma Gondii Gt1

TISSUE(S): Cell Culture

SUBMITTER: Yongle Song

LAB HEAD: Yanqin Zhou

PROVIDER: PXD032102 | Pride | 2022-09-25

REPOSITORIES: Pride

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			Action	DRS
	20170301_YS_BirA-1__F008319_.mzid.gz	Mzid
	20170301_YS_BirA-1__F008319_.mzid_20170301_YS_BirA-1__F008319_.MGF	Mzid
	20170301_YS_BirA-2__F008320_.mzid.gz	Mzid
	20170301_YS_BirA-2__F008320_.mzid_20170301_YS_BirA-2__F008320_.MGF	Mzid
	20170301_YS_BirA-3__F008332_.mzid.gz	Mzid

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