Proteomic analysis identifies endoribouclease EhL-PSP and EhRRP41 exosome protein as novel interactors of EhCAF1 deadenylase

López-Rosas, Itzel; Marchat, Laurence A.; Olvera, Beatriz Gallo; Guillén, Nancy; Weber, Christian; Cruz, Olga Hernández de la; Ruiz-García, Érika; Vega, Horacio Astudillo‐de la; López-Camarillo, César

doi:10.1016/j.jprot.2014.06.019

Cited by 13 publications

(13 citation statements)

References 67 publications

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“…Given the above information and the speculation that Rhp-PSP also possesses the properties of an endoribonuclease L-PSP, we hypothesised that Rhp-PSP may exert its anti-TMV activity through the degradation of the RNA of this positive-sense single-stranded RNA virus. However, the study related to the endoribonucleolytic activities of the YER057c/YjgF/UK114 family is minimal and limited to the homologues from humans, rats, goats, and the newly reported EhL-PSP from Entamoeba histolytica 37 . The R. palustris -produced endoribonuclease L-PSP has not yet been characterized.…”

Section: Discussionmentioning

confidence: 99%

Isolation of Rhp-PSP, a member of YER057c/YjgF/UK114 protein family with antiviral properties, from the photosynthetic bacterium Rhodopseudomonas palustris strain JSC-3b

Feng

Zhou

et al. 2015

Sci Rep

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Rhodopseudomonas palustris strain JSC-3b isolated from a water canal adjacent to a vegetable field produces a protein that was purified by bioactivity-guided fractionation based on ammonium sulfate precipitation, ion-exchange absorption and size exclusion. The protein was further identified as an endoribonuclease L-PSP (Liver-Perchloric acid-soluble protein) by shotgun mass spectrometry analysis and gene identification, and it is member of YER057c/YjgF/UK114 protein family. Herein, this protein is designated Rhp-PSP. Rhp-PSP exhibited significant inhibitory activities against tobacco mosaic virus (TMV) in vivo and in vitro. To our knowledge, this represents the first report on the antiviral activity of a protein of the YER057c/YjgF/UK114 family and also the first antiviral protein isolated from R. palustris. Our research provides insight into the potential of photosynthetic bacterial resources in biological control of plant virus diseases and sustainable agriculture.

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Section: Discussionmentioning

confidence: 99%

Isolation of Rhp-PSP, a member of YER057c/YjgF/UK114 protein family with antiviral properties, from the photosynthetic bacterium Rhodopseudomonas palustris strain JSC-3b

Feng

Zhou

et al. 2015

Sci Rep

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“…The concentration of protein was determined by the BCA assay. Co-IP was performed according to a previous study (18). Briefly, 10 µ g of rabbit anti-HO-1 anti-body was added into 1 mg supernatants of 293T/HO-1 cells and then incubated overnight at 4°C.…”

Section: Methodsmentioning

confidence: 99%

HO-1/EBP interaction alleviates cholesterol-induced hypoxia through the activation of the AKT and Nrf2/mTOR pathways and inhibition of carbohydrate metabolism in cardiomyocytes

Jin

Cao

et al. 2017

International Journal of Molecular Medicine

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Heme oxygenase-1 (HO-1) is an inducible and cytoprotective enzyme that provides a defense against oxidant damage. The present study screened 137 HO-1/interacting proteins using a profound co-immunoprecipitation (Co-IP) coupled with proteomics, and profiled the global HO-1 interactome network, including oxidative phosphorylation, endoplasmic reticulum and transport vesicle functions. Among these molecules, we observed that a novel interactor, emopamil-binding protein (EBP), is closely related to the cholesterol metabolism process. This study demonstrated that cholesterol promotes excessive oxidative stress and alters the energy metabolism in cardiomyocytes, further triggering numerous cardiovascular diseases. We observed that cholesterol caused the overexpression of EBP and HO-1 by the activation of AKT and Nrf2/mTOR pathways. In addition, HO-1 and EBP performed a myocardial protective function. The overexpression of HO-1 alleviated the cholesterol-induced excessive oxidative stress status by inhibition of the carbohydrate metabolism. Notably, we also confirmed that the loss of partial HO-1 activity aggravated the oxidative damage and cardiac systolic function induced by a high-fat diet in HO-1 heterozygous (HO-1+/−) mice. These findings indicate that the HO-1/EBP interaction plays a protective role in alleviating the dysfunction of oxidative stress and cardiac systolic function induced by cholesterol stimulation.

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“…EhCAF1 is a ribonuclease D family member, having the CAF1 nuclease domain and the conserved DEDD residues (D 84 E 86 D 206 D 276 ) that are important for 3′ to 5′ exonuclease activity in homologous proteins (Daugeron et al, 2001 ). Consequently, EhCAF1 is a functional deadenylase that binds 3′UTR and degrades the poly(A) tail of parasite transcripts in in vitro assays (López-Rosas et al, 2014 ).…”

Section: Molecular Events For Mrna Decay In E Histolytica mentioning

confidence: 99%

“…Then, DCP2 mRNA decapping enzyme removes the cap structure from the 5′ end of the mRNA with the help of accessories proteins Edc3 and Dhh1, which allows 5′-3′ exoribonuclease XRN2 with Lsm protein complex to degrade the rest of mRNA body. Alternatively, the deadenylated transcript is degraded in a 3′-5′ direction by the catalytic subunit Dis3 of the exosome complex and the cap structure is eliminated by DCPs protein (López-Rosas et al, 2012 , 2014 ).…”

Section: Molecular Events For Mrna Decay In E Histolytica mentioning

confidence: 99%

Life and Death of mRNA Molecules in Entamoeba histolytica

Valdés-Flores

López-Rosas

López-Camarillo

et al. 2018

Front. Cell. Infect. Microbiol.

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In eukaryotic cells, the life cycle of mRNA molecules is modulated in response to environmental signals and cell-cell communication in order to support cellular homeostasis. Capping, splicing and polyadenylation in the nucleus lead to the formation of transcripts that are suitable for translation in cytoplasm, until mRNA decay occurs in P-bodies. Although pre-mRNA processing and degradation mechanisms have usually been studied separately, they occur simultaneously and in a coordinated manner through protein-protein interactions, maintaining the integrity of gene expression. In the past few years, the availability of the genome sequence of Entamoeba histolytica, the protozoan parasite responsible for human amoebiasis, coupled to the development of the so-called “omics” technologies provided new opportunities for the study of mRNA processing and turnover in this pathogen. Here, we review the current knowledge about the molecular basis for splicing, 3′ end formation and mRNA degradation in amoeba, which suggest the conservation of events related to mRNA life throughout evolution. We also present the functional characterization of some key proteins and describe some interactions that indicate the relevance of cooperative regulatory events for gene expression in this human parasite.

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Proteomic analysis identifies endoribouclease EhL-PSP and EhRRP41 exosome protein as novel interactors of EhCAF1 deadenylase

Cited by 13 publications

References 67 publications

Isolation of Rhp-PSP, a member of YER057c/YjgF/UK114 protein family with antiviral properties, from the photosynthetic bacterium Rhodopseudomonas palustris strain JSC-3b

Isolation of Rhp-PSP, a member of YER057c/YjgF/UK114 protein family with antiviral properties, from the photosynthetic bacterium Rhodopseudomonas palustris strain JSC-3b

HO-1/EBP interaction alleviates cholesterol-induced hypoxia through the activation of the AKT and Nrf2/mTOR pathways and inhibition of carbohydrate metabolism in cardiomyocytes

Life and Death of mRNA Molecules in Entamoeba histolytica

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