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Toxoplasma gondii Tgj1 Hsp40 protein interaction LC-MS/MS

ABSTRACT: We identified an Hsp40 Ydj1 / Hdj2 ortholog in T. gondii, which is involved in various biological roles in T. gondii as deduced from its interactome and analysis of the ΔCXXX mutant. Among these roles are differentiation and DNA damage, as well as metabolic pathways such as translation and energy generation.

INSTRUMENT(S):

ORGANISM(S): Toxoplasma Gondii

TISSUE(S): Cell Culture

SUBMITTER: BIN DENG

LAB HEAD: Bin Deng

PROVIDER: PXD024656 | Pride | 2023-05-10

REPOSITORIES: Pride

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			Action	DRS
	QE_2018_0034-Sample1.msf	Msf
	QE_2018_0034-Sample1.raw	Raw
	QE_2018_0035_Sample2.msf	Msf
	QE_2018_0035_Sample2.raw	Raw
	QE_2018_0036_Sample3.msf	Msf

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Publications

Analysis of the Interactome of the Toxoplasma gondii Tgj1 HSP40 Chaperone.

Munera López Jonathan J Alonso Andrés Mariano AM Figueras Maria Julia MJ Saldarriaga Cartagena Ana María AM Hortua Triana Miryam A MA Diambra Luis L Vanagas Laura L Deng Bin B Moreno Silvia N J SNJ Angel Sergio Oscar SO

Proteomes 20230301 1

Toxoplasma gondii is an obligate intracellular apicomplexan that causes toxoplasmosis in humans and animals. Central to its dissemination and pathogenicity is the ability to rapidly divide in the tachyzoite stage and infect any type of nucleated cell. Adaptation to different cell contexts requires high plasticity in which heat shock proteins (Hsps) could play a fundamental role. Tgj1 is a type I Hsp40 of T. gondii, an ortholog of the DNAJA1 group, which is essential during the tach ...[more]

PMID: 36976888

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Acetylation of the yeast Hsp40 chaperone protein Ydj1 regulates proteostasis and translational fidelity

Project description:In this study, we set out to clarify the role of lysine acetylation on the major yeast Hsp40, Ydj1. We mutated a series of acetylation sites on Ydj1s J domain to either arginine to block acetylation or glutamine to mimic constitutive acetylation.

2024-04-14 | MSV000094536 | MassIVE

The HSP40 chaperone Ydj1/DnaJA1 drives amyloid beta toxicity

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2022-04-27 | PXD012612 | Pride

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Genome-wide cooperation by HAT Gcn5, remodeler SWI/SNF, and chaperone Ydj1 in promoter nucleosome eviction and transcriptional activation

Project description:Chaperones, nucleosome remodeling complexes and histone acetyltransferases have been implicated in nucleosome disassembly at promoters of particular yeast genes, but whether these co-factors function ubiquitously, and the impact of nucleosome eviction on transcription genome-wide, are poorly understood. We used chromatin immunoprecipitation of histone H3 and RNA polymerase II (Pol II) in mutants lacking single or multiple co-factors to address these issues for ~200 genes belonging to the Gcn4 transcriptome, of which ~70 exhibit marked reductions in H3 promoter occupancy on induction by amino acid starvation. Examining four target genes in a panel of mutants indicated that SWI/SNF, Gcn5, the Hsp70 co-chaperone Ydj1, and chromatin-associated factor Yta7 are required downstream of Gcn4 binding for robust H3 eviction in otherwise wild-type cells. Using ChIP-seq to interrogate all 70 exemplar genes in single, double and triple mutants implicated Gcn5, Snf2 and Ydj1 in H3 eviction at most, but not all Gcn4 target promoters, with Gcn5 generally playing the greatest role and Ydj1 the least. Remarkably, these 3 co-factors cooperate similarly in H3 eviction at virtually all yeast promoters. Defective H3 eviction in co-factor mutants was coupled with reduced Pol II occupancies for the Gcn4 transcriptome and the most highly expressed uninduced genes, but the relative Pol II levels at most genes were unaffected or even elevated. These findings indicate that nucleosome eviction is crucial for robust transcription of highly expressed genes, but that other steps in gene activation are more rate-limiting for most other yeast genes. Chromatin immunoprecipitated DNA from WT (induced(+SM) and uninduced(no SM)) and mutants (induced(+SM)) followed by paired-end sequencing. Nucleosomal DNA obtained by MNase digestion were also subjected to paired-end sequencing.

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Rsp5/Nedd4 is the major ubiquitin ligase that targets cytosolic misfolded proteins upon heat-stress

Project description:The heat-shock response is a complex cellular program that induces major changes in protein translation, folding and degradation to alleviate toxicity caused by protein misfolding. While heat-shock has been widely used to study proteostasis, it remained unclear how misfolded proteins are targeted for proteolysis in these conditions. We found that Rsp5 and its mammalian homologue Nedd4 are the main E3-ligases responsible for the increased ubiquitination induced by heat-stress. We determined that Rsp5 ubiquitinates cytosolic misfolded proteins upon heat-shock for proteasome degradation. We found that ubiquitination of heat-induced substrates requires the Hsp40 co-chaperone Ydj1 that is further associated with Rsp5 upon heat-shock. Additionally, ubiquitination is also promoted by PY Rsp5-binding motifs found primarily in the structured regions of stress-induced substrates, which can act as heat-induced degrons. Our results support a bipartite recognition mechanism combining direct and chaperone-dependent ubiquitination of misfolded cytosolic proteins by Rsp5.

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Structural probing of Hsp26 activation and client binding by quantitative cross-linking mass spectrometry

Project description:Small heat-shock proteins (sHSP) are important members of the cellular stress response in all species. Their best described function is the binding of early unfolding states and the resulting prevention of protein aggregation. All sHSPs exist as oligomers but vary in size and subunit organization. Some sHSPs exist as a polydisperse composition of oligomers which undergoes changes in subunit composition, folding status and relative distribution upon heat activation. To date only an incomplete picture of the mechanism of sHSP activation exists and in particularly the molecular basis of how sHSPs bind client proteins and mediate client specificity is not fully understood. In this study we have applied cross-linking mass spectrometry (XL-MS) to obtain detailed structural information on sHSP activation and client binding for yeast Hsp26. Our cross-linking data reveals the middle domain of Hsp26 as client-independent interface in multiple Hsp26::client complexes and indicates that client-specificity is likely mediated via additional binding sites with its αCD and CTE. Our quantitative XL-MS data underpins the middle domain as the main driver of heat-induced activation and client binding but shows that global rearrangements spanning all domains of Hsp26 are taking place simultaneously. We also investigated a Hsp26::client complex in the presence of Ssa1 (Hsp70) and Ydj1(Hsp40) at the initial stage of refolding and see that the interaction between refolding chaperones is altered by the presence of a client protein, pointing to a mechanism where interaction of Ydj1 with the HSP::client complex initiates assembly of the active refolding machinery.

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Comparative characterization of microRNA profiles of different genotypes of Toxoplasma gondii

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