A common signalosome for programmed cell death in humans and plants

Martínez-Fábregas, Jonathan; Dı́az-Moreno, Irene; González‐Arzola, Katiuska; Díaz-Quintana, Antonio; Rosa, Miguel Á. De la

doi:10.1038/cddis.2014.280

Cited by 43 publications

(61 citation statements)

References 8 publications

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“…NMR assignments of the 15 . CSP titration curves were analyzed using one-site and two-site binding models, as previously described [29].…”

Section: Nmr Measurementsmentioning

confidence: 99%

“…15 N-labeled hCc was expressed in M9 minimal medium for Nuclear Magnetic Resonance (NMR) titrations, whereas unlabeled hCc was produced in Luria-Bertani (LB) medium for Isothermal Titration Calorimetry (ITC) measurements. Expression and purification protocol was similar to that recently described for pCc [29], excepting the cell culture was at 30°C and the elution gradient for the cationic exchange column, which ranged from 0.036 to 0.36 M NaCl.…”

Section: Protein Expression and Purificationmentioning

confidence: 99%

“…CSP titration curves were analyzed using one-site and two-site binding models, as previously described [29]. Additionally, 15 N-labeled hCc red and unlabeled pCc1 red at a ratio of 1:2, was titrated with increasing concentrations of NaCl. Each titration step was prepared in the same tube and the pH of the samples was also checked for each spectrum.…”

Section: Nmr Measurementsmentioning

confidence: 99%

“…The organization of the mitochondrial electron transport chain is a subject of intense debate at present, where two different models are being considered: the fluid model, that proposes a random organization for individual respiratory protein components, and the solid model, suggesting a stable association between individual complexes [6][7][8]. Apart their role in respiration, Cc and Cc 1 are clearly involved in the development of programmed cell death [9][10][11][12][13][14][15]. Such a dual role of Cc is regulated by post-translational modifications -namely, phosphorylation and nitration of tyrosine residues -that affect the binding of Cc to its physiological counterparts, either in the mitochondria or in the cytoplasm [16][17][18][19][20][21][22][23].…”

Section: Introductionmentioning

confidence: 99%

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Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

et al. 2015

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a b s t r a c tThe transient interactions of respiratory cytochrome c with complexes III and IV is herein investigated by using heterologous proteins, namely human cytochrome c, the soluble domain of plant cytochrome c 1 and bovine cytochrome c oxidase. The binding molecular mechanisms of the resulting cross-complexes have been analyzed by Nuclear Magnetic Resonance and Isothermal Titration Calorimetry. Our data reveal that the two cytochrome c-involving adducts possess a 2:1 stoichiometry -that is, two cytochrome c molecules per adduct -at low ionic strength. We conclude that such extra binding sites at the surfaces of complexes III and IV can facilitate the turnover and sliding of cytochrome c molecules and, therefore, the electron transfer within respiratory supercomplexes.

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“…NMR assignments of the 15 . CSP titration curves were analyzed using one-site and two-site binding models, as previously described [29].…”

Section: Nmr Measurementsmentioning

confidence: 99%

Section: Protein Expression and Purificationmentioning

confidence: 99%

Section: Nmr Measurementsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

et al. 2015

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“…Recently, SET/TAF-1β was found to be recruited to DNA breaks to modulate the DNA damage response through the retention of certain chromatin proteins, resulting in chromatin compaction (16). We have identified SET/TAF-Iβ as a target protein for cytochrome c (Cc) following the release of the latter from mitochondria in human cells treated with apoptotic agents (17,18). Although the hemeprotein Cc serves as an electron carrier between complexes III and IV in the mitochondrial respiratory chain, its role in nuclei has yet to be convincingly elucidated.…”

mentioning

confidence: 99%

Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochromec

González‐Arzola

Dı́az-Moreno

Cano-González

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

119

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Chromatin is pivotal for regulation of the DNA damage process insofar as it influences access to DNA and serves as a DNA repair docking site. Recent works identify histone chaperones as key regulators of damaged chromatin’s transcriptional activity. However, understanding how chaperones are modulated during DNA damage response is still challenging. This study reveals that the histone chaperone SET/TAF-Iβ interacts with cytochrome c following DNA damage. Specifically, cytochrome c is shown to be translocated into cell nuclei upon induction of DNA damage, but not upon stimulation of the death receptor or stress-induced pathways. Cytochrome c was found to competitively hinder binding of SET/TAF-Iβ to core histones, thereby locking its histone-binding domains and inhibiting its nucleosome assembly activity. In addition, we have used NMR spectroscopy, calorimetry, mutagenesis, and molecular docking to provide an insight into the structural features of the formation of the complex between cytochrome c and SET/TAF-Iβ. Overall, these findings establish a framework for understanding the molecular basis of cytochrome c-mediated blocking of SET/TAF-Iβ, which subsequently may facilitate the development of new drugs to silence the oncogenic effect of SET/TAF-Iβ’s histone chaperone activity.

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Nuclear cytochrome c – a mitochondrial visitor regulating damaged chromatin dynamics

et al. 2018

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Over the past decade, evidence has emerged suggesting a broader role for cytochrome c (Cyt c) in programmed cell death. Recently, we demonstrated the ability of Cyt c to inhibit the nucleosome assembly activity of histone chaperones SET/template-activating factor Iβ and NAP1-related protein during DNA damage in humans and plants respectively. Here, we hypothesise a dual concentration-dependent function for nuclear Cyt c in response to DNA damage. We propose that low levels of highly cytotoxic DNA lesions - such as double-strand breaks - induce nuclear translocation of Cyt c, leading to the attenuation of nucleosome assembly and, thereby, increasing the time available for DNA repair. If DNA damage persists or is exacerbated, the nuclear Cyt c concentration would exceed a given threshold, causing the haem protein to block DNA remodelling altogether.

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A common signalosome for programmed cell death in humans and plants

Cited by 43 publications

References 8 publications

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

Structural basis for inhibition of the histone chaperone activity of SET/TAF-Iβ by cytochromec

Nuclear cytochrome c – a mitochondrial visitor regulating damaged chromatin dynamics

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