Zim17/Tim15 links mitochondrial iron–sulfur cluster biosynthesis to nuclear genome stability
|Author||Díaz de la Loza, María del Carmen
Gallardo Ortega, Mercedes
García Rubio, María Luisa
Aguilera López, Andrés
Wellinger, Ralf Erik
|Department||Universidad de Sevilla. Departamento de Genética|
|Abstract||Genomic instability is related to a wide-range of human diseases. Here, we show that mitochondrial iron–sulfur cluster biosynthesis is important for the maintenance of nuclear genome stability in Saccharomyces cerevisiae. ...
Genomic instability is related to a wide-range of human diseases. Here, we show that mitochondrial iron–sulfur cluster biosynthesis is important for the maintenance of nuclear genome stability in Saccharomyces cerevisiae. Cells lacking the mitochondrial chaperone Zim17 (Tim15/Hep1), a component of the iron–sulfur biosynthesis machinery, have limited respiration activity, mimic the metabolic response to iron starvation and suffer a dramatic increase in nuclear genome recombination. Increased oxidative damage or deficient DNA repair do not account for the observed genomic hyperrecombination. Impaired cell-cycle progression and genetic interactions of ZIM17 with components of the RFC-like complex involved in mitotic checkpoints indicate that replicative stress causes hyperrecombination in zim17Δ mutants. Furthermore, nuclear accumulation of pre-ribosomal particles in zim17Δ mutants reinforces the importance of iron–sulfur clusters in normal ribosome biosynthesis. We propose that compromised ribosome biosynthesis and cell-cycle progression are interconnected, together contributing to replicative stress and nuclear genome instability in zim17Δ mutants.
|Funding agencies||Ministerio de Ciencia e Innovación (MICIN). España
Junta de Andalucía
|Citation||Díaz de la Loza, M.d.C., Gallardo Ortega, M., García Rubio, M.L., Izquierdo, A., Herrero, E., Aguilera López, A. y Wellinger, R.E. (2011). Zim17/Tim15 links mitochondrial iron–sulfur cluster biosynthesis to nuclear genome stability. Nucleic Acids Research, 39 (14), 6002-6015.|
This item appears in the following collection(s)
Except where otherwise noted, this item's license is described as: Attribution-NonCommercial-NoDerivatives 4.0 Internacional
Showing items related by title, author, creator and subject.
A Universal Stress Protein Involved in Oxidative Stress Is a Phosphorylation Target for Protein Kinase CIPK6 Torre Fazio, Fernando de la; Pozo Cañas, Olga del; Personat, José María; Gutiérrez Beltrán, Emilio (American Society of Plant Biologists, 2017)
Calcineurin B-like interacting protein kinases (CIPKs) decode calcium signals upon interaction with the calcium sensors ...
Induction of the nitrate assimilation nira operon and protein-protein interactions in the maturation of nitrate and nitrite reductases in the cyanobacterium Anabaena sp. strain PCC 7120 Frías Sánchez, José Enrique; Flores García, Enrique (American Society for Microbiology, 2015-07)
Nitrate is widely used as a nitrogen source by cyanobacteria, in which the nitrate assimilation structural genes frequently ...
Goder, Veit; Melero, Alejandro (Company of Biologists Ltd, 2011)
In eukaryotic cells, proteins enter the secretory pathway at the endoplasmic reticulum (ER) as linear polypeptides and ...