The trypanosomal orthologue of the mitoribosome receptor Mba1 (TbMba1) is essential for normal growth of procyclic trypanosomes. Proteomic analyses of TbMba1-depleted mitochondria revealed reduced levels of many components of the cytochrome c oxidase (Cox) complex, three subunits of which are mitochondrially encoded. Pull-down experiments showed that TbMba1 forms a dynamic interaction network that includes the trypanosomal Mdm38/Letm1 orthologue and a trypanosome-specific factor that stabilizes the CoxI and CoxII mRNAs.

The genetic code expansion technique generates site-specifically acetylated proteins for studying lysine acetylation of citric acid cycle enzymes, including the impacts on enzyme activities, acetylation mechanisms, and deacetylase specificities.

The two phenazines retained in Pseudomonas aeruginosa biofilms, PYO and PCN, are primarily reduced in different cellular compartments: PYO mainly in the cytosol, PCN mainly at the inner membrane by the Nqr complex.

C. albicans possess both canonical and variant histone H3, and evolutionarily conserved histone H3 chaperone complexes, CAF-1 and HIR. The question remains whether both the histone chaperones assist the loading of histones or specific chaperones are designated for canonical and histone variants. While the CAF-1 complex is known to act as a major chaperone for canonical histone H3 loading, our studies suggest that it might act as a chaperone for variant histone H3, H3V^CTG in C. albicans.

We reveal the molecular details of how the sensor lipoprotein NlpE activates the Cpx two-component stress response. Through complementary genetics, biochemistry, and AlphaFold2 modeling, we identified NlpE residues that are critical for binding the CpxA histidine kinase in the periplasm and activating the response. We also identify CpxA residues required for NlpE interaction. Remarkably, CpxA variants that are blinded to NlpE can respond to other stressors, showing that CpxA can uniquely recognize stress signals.

The model cyanobacterium, Synechocystis sp. PCC 6803, switches between a planktonic and a biofilm lifestyle in response to fluctuating environmental conditions. The two-component regulatory systems, Hik12-Rre2 and Hik14-Rre8, function in biofilm formation during high salt stress. Both response regulators, Rre2 and Rre8 catalyze the production of c-di-GMP and are involved in this process.

In this study, we show that the transcription factor Pathogenicity factor 2 (Pf2) is a positive regulator of the fungal necrotrophic effector ToxB within the global wheat pathogen Pyrenophora tritici-repentis (Ptr). We investigate the function of Pf2 in different Ptr races via profiling of the secreted fungal proteins and examine the significant promoter motifs identified via GFP report assays.

In yeast but not plant and animal systems, the rapid degradation of transcripts with premature termination codon is dependent on mRNA decapping and the cytoplasmic exonuclease, Xrn1. We show the fungus, Aspergillus nidulans does not fit the yeast model, suggesting as yet unidentified RNA degradation mechanisms are involved. Surprisingly, disruption specifically of the regulatory component of the decapping complex, Dcp1, leads to an accumulation of rRNA degradation products.

The apoptosis-inducing factor (AIF) present in the protoplasm of the Entamoeba histolytica trophozoites, migrates to the nucleus when the trophozoites are stressed with heat shock, oxidative shock or drug treatment. Once the AIF is in the nucleus, they cause the peripheral chromosome condensation and DNA degradation. These ultimately lead to the apoptosis of the E. histolytica, the pathogen of amoebiasis.