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Interactome identification of Histones H3 and H4 in the presence and absence of methyl methanesulfonate (MMS) in the pathogenic yeast Candida glabrata

ABSTRACT: The main goal of this project is to identify proteins in Candida glabrata that interact with histones H3 (CgHht) and H4 (CgHhf) under normal and MMS-treatment conditions.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Candida Glabrata (yeast) (torulopsis Glabrata)

SUBMITTER: Rupinder Kaur

LAB HEAD: Dr. Rupinder Kaur

PROVIDER: PXD016867 | Pride | 2020-02-21

REPOSITORIES: Pride

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Publications

Histone H4 dosage modulates DNA damage response in the pathogenic yeast Candida glabrata via homologous recombination pathway.

Kumar Kundan K Moirangthem Romila R Kaur Rupinder R

PLoS genetics 20200305 3

Candida glabrata, a nosocomial fungal bloodstream pathogen, causes significant morbidity and mortality in hospitals worldwide. The ability to replicate in macrophages and survive a high level of oxidative stress contributes to its virulence in the mammalian host. However, the role of DNA repair and recombination mechanisms in its pathobiology is still being discovered. Here, we have characterized the response of C. glabrata to the methyl methanesulfonate (MMS)-induced DNA damage. We found that t ...[more]

PMID: 32134928

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Interactome analysis of the CgHog1 MAPK under varied-iron conditions in Candida glabrata

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Truncated PARP1 promotes RNA Polymerase III during apoptosis

Project description:The N-terminal three zinc finger motifs of PARP1 are evolutionarily conserved in multicellular organism。However, during apoptosis, human PARP1 is mainly cleaved by caspase 3 at D214. As a result, the truncated PARP1 loses two N-terminal zinc finger motifs and only contains the third zinc finger motif, the BRCT domain, the WGR domain and the C-terminal catalytic domain. Interestingly, when we explored the domain architecture of PARP1 in other organisms, we found that similar to human tPARP1, PARP1 orthologs in several lower organisms do not have the N-terminal two zinc fingers or even they lack the third zinc finger motif. It indicates that even without the first two zinc finger motifs, tPARP1 may still catalyze ADP-ribosylation and play an important role in certain biological processes. To reveal the biological function of tPARP1, we performed tandem affinity purification and searched for the possible substrates.

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The SAM domain-containing protein 1 (SAMD1) acts as a repressive chromatin regulator at unmethylated CpG islands

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