Subcellular Localization of Fad1p in Saccharomyces cerevisiae: A Choice at Post-Transcriptional Level?

Autor: Francesco Bruni, Teresa Anna Giancaspero, Mislav Oreb, Maria Tolomeo, Piero Leone, Eckhard Boles, Marina Roberti, Michele Caselle, Maria Barile

Publikováno v: Life, Vol 11, Iss 9, p 967 (2021)

FAD synthase is the last enzyme in the pathway that converts riboflavin into FAD. In Saccharomyces cerevisiae, the gene encoding for FAD synthase is FAD1, from which a sole protein product (Fad1p) is expected to be generated. In this work, we showed

Externí odkaz: https://doaj.org/article/e5697caf7b5544678c19ce5c772586fb

FAD synthesis and degradation in the nucleus create a local flavin cofactor pool

Autor: Teresa Anna Giancaspero, Grazia Maria Liuzzi, Angelica Miccolis, Giovanni Busco, Claudia Carmone, Concetta Panebianco, Maria Barile, Matilde Colella

Publikováno v: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2013, 288 (40), pp.29069-29080. ⟨10.1074/jbc.M113.500066⟩
Europe PubMed Central
Journal of biological chemistry (Online) 288 (2013): 29069.
info:cnr-pdr/source/autori:Giancaspero T. A., Busco G., Panebianco C., Carmone C., Miccolis A., Liuzzi G.M., Colella M., Barile M./titolo:FAD Synthesis and Degradation in the Nucleus Create a Local Flavin Cofactor Pool/doi:/rivista:Journal of biological chemistry (Online)/anno:2013/pagina_da:29069/pagina_a:/intervallo_pagine:29069/volume:288
Journal of Biological Chemistry, 288, 29069-80
Journal of Biological Chemistry, 288, 40, pp. 29069-80

Background: FAD synthase is known to catalyze the biosynthesis of FAD in cytosol and mitochondria. Results: The existence of a nuclear FAD synthase and a FAD-hydrolyzing activity is demonstrated. Conclusion: A dynamic pool of FAD exists in the nucleu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07dfc13384011936d24ef3238cb8016f
https://doi.org/10.1074/jbc.M113.500066

Bacterial Over-Expression and Purification of the 3′phosphoadenosine 5′phosphosulfate (PAPS) Reductase Domain of Human FAD Synthase: Functional Characterization and Homology Modeling

Autor: Cesare Indiveri, Angelica Miccolis, Teresa Anna Giancaspero, Maria Barile, Michele Galluccio

Publikováno v: International Journal of Molecular Sciences
International Journal of Molecular Sciences; Volume 13; Issue 12; Pages: 16880-16898

FAD synthase (FADS, EC 2.7.7.2) is a key enzyme in the metabolic pathway that converts riboflavin into the redox cofactor, FAD. Human FADS is organized in two domains: -the 3'phosphoadenosine 5'phosphosulfate (PAPS) reductase domain, similar to yeast

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b7152e027bbc9849a45b2f38e7b660e
http://europepmc.org/articles/PMC3546728

Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins

Autor: Teresa Anna Giancaspero, Michele Galluccio, Cesare Indiveri, Maria Barile, Stefania Iametti, Elisabetta Gianazza, Enza Maria Torchetti, Francesco Bonomi

Publikováno v: FEBS Journal. 278:4434-4449

A soluble form of human FAD synthase (isoform 2; hFADS2) was produced and purified to homogeneity as a recombinant His-tagged protein. The enzyme binds 1 mole of the FAD product very tightly, although noncovalently. Complete release of FAD from the '

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d74f5e7a9dbdbb167d443a83a4bbfac5
https://doi.org/10.1111/j.1742-4658.2011.08368.x

Succinate dehydrogenase flavoprotein subunit expression in Saccharomyces cerevisiae- involvement of the mitochondrial FAD transporter, Flx1p

Autor: Eckhard Boles, Teresa Anna Giancaspero, Robin Wait, Maria Barile

Publikováno v: FEBS Journal. 275:1103-1117

The mitochondrial FAD transporter, Flx1p, is a member of the mitochondrial carrier family responsible for FAD transport in Saccharomyces cerevisiae. It has also been suggested that it has a role in maintaining the normal activity of mitochondrial FAD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::d408118167098b59ada9811588a3ee35
https://doi.org/10.1111/j.1742-4658.2008.06270.x