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During its complex life cycle, the malaria parasite survives dramatic environmental stresses, including large temperature shifts. Protein prenylation is required during asexual replication of Plasmodium falciparum, and the canonical heat shock protein 40 protein (HSP40; PF3D7_1437900) is posttranslationally modified with a 15-carbon farnesyl isoprenyl group. In other organisms, farnesylation of Hsp40 orthologs controls their localization and function in resisting environmental stress. In this work, we find that plastidial isopentenyl pyrophosphate (IPP) synthesis and protein farnesylation are required for malaria parasite survival after cold and heat shock. Furthermore, loss of HSP40 farnesylation alters its membrane attachment and interaction with proteins in essential pathways in the parasite. Together, this work reveals that farnesylation is essential for parasite survival during temperature stress. Farnesylation of HSP40 may promote thermotolerance by guiding distinct chaperone-client protein interactions.
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http://dx.doi.org/10.1128/mBio.00760-21 | DOI Listing |
J Cell Mol Med
December 2024
Cardiovascular Center, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Fibrosis, characterised by excessive extracellular matrix deposition, contributes to both organ failure and significant mortality worldwide. Whereas fibroblasts are activated into myofibroblasts, marked by phenotypic factors such as α-smooth muscle actin (α-SMA), periostin, fibroblast activation protein (FAP) and heat shock protein 47 (HSP47), the cellular processes of trans-differentiation for fibrosis development remain poorly understood. Herein, we hypothesised that the molecular signalling of geranylgeranyl pyrophosphate (GGPP), a crucial biochemical molecule for protein prenylation, is essential in the regulation of profibrotic mechanisms for fibroblast-to-myofibroblast activation.
View Article and Find Full Text PDFChem Biol Interact
December 2024
Department of Food Science and Biotechnology, Andong National University, Andong, 36729, Republic of Korea. Electronic address:
Prenylation, which involves the addition of hydrophobic molecules, is considered to enhance the bioavailability and biological activity of flavonoids. However, the effect of prenylation on the estrogenic activity of flavonoids with different structures remains unclear. This study evaluated the estrogen receptor-α (ER-α) agonistic and antagonistic activities of estrogenic flavonoids in both unprenylated and prenylated forms using OECD standardized in vitro ER-α transactivation assay and in vivo uterine hypertrophy assay.
View Article and Find Full Text PDFBiochemistry
December 2024
Department of Chemistry, University of Minnesota-Twin Cities, Minneapolis, Minnesota 55455, United States.
Prenylation consists of the modification of proteins with either farnesyl diphosphate (FPP) or geranylgeranyl diphosphate (GGPP) at a cysteine near the C-terminus of target proteins to generate thioether-linked lipidated proteins. In recent work, metabolic labeling with alkyne-containing isoprenoid analogues including C15AlkOPP has been used to identify prenylated proteins and track their levels in different diseases. Here, a systematic study of the impact of isoprenoid length on proteins labeled with these probes was performed.
View Article and Find Full Text PDFMethods Enzymol
November 2024
Centre for Environmental Biotechnology, School of Environmental and Natural Sciences, Bangor University, Bangor, United Kingdom; Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Canada. Electronic address:
Microbial carboxylases and decarboxylases play important roles in the global carbon cycle and have many potential applications in biocatalysis and synthetic biology. The widespread family of reversible UbiD-like (de)carboxylases are of particular interest because these enzymes are active against a diverse range of substrates. Several characterized UbiD enzymes have been shown to catalyze reversible (de)carboxylation of aromatic and aliphatic substrates using the recently discovered prenylated FMN (prFMN) cofactor, which is produced by the associated family of UbiX FMN prenyltransferases.
View Article and Find Full Text PDFVirulence
December 2024
Xinxiang Key Laboratory of Pathogenic Biology, Department of Pathogenic Biology, School of Basic Medical Sciences, Xinxiang Medical University, Xinxiang, Henan, PR China.
Prenyltransferases act essential roles in the prenylation modification, which is significant for proteins, like small GTPases to execute various important activities in (). The structures and partial functions of prenyltransferases (FTase, GGTase-I, and GGTase-II) in prenylation process have been dissected in . However, the cellular effects of prenyltransferases on type 2-ME49 strain of are largely unknown.
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