Mapping of the interaction domain for purified cytochrome c1 on cytochrome c

König, B.W.; Osheroff, Neil; Wilms, J.; Muijsers, Anton O.; Dekker, H.; Margoliash, E.

doi:10.1016/0014-5793(80)80835-0

Cited by 78 publications

(26 citation statements)

References 13 publications

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“…This latter finding is in agreement with previous works in which lysine residues were found to be involved in the binding of C c to cytochrome b c 1 (44,68,71,72), cytochrome c oxidase (67) and GALDH (49), as well as to partners in apoptosis like Apaf-1 (73) and SET/TAF-Iβ (40). …”

Section: Resultssupporting

confidence: 93%

Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c

González‐Arzola

Díaz‐Quintana

Rivero-Rodríguez

et al. 2016

Nucleic Acids Research

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Higher-order plants and mammals use similar mechanisms to repair and tolerate oxidative DNA damage. Most studies on the DNA repair process have focused on yeast and mammals, in which histone chaperone-mediated nucleosome disassembly/reassembly is essential for DNA to be accessible to repair machinery. However, little is known about the specific role and modulation of histone chaperones in the context of DNA damage in plants. Here, the histone chaperone NRP1, which is closely related to human SET/TAF-Iβ, was found to exhibit nucleosome assembly activity in vitro and to accumulate in the chromatin of Arabidopsis thaliana after DNA breaks. In addition, this work establishes that NRP1 binds to cytochrome c, thereby preventing the former from binding to histones. Since NRP1 interacts with cytochrome c at its earmuff domain, that is, its histone-binding domain, cytochrome c thus competes with core histones and hampers the activity of NRP1 as a histone chaperone. Altogether, the results obtained indicate that the underlying molecular mechanisms in nucleosome disassembly/reassembly are highly conserved throughout evolution, as inferred from the similar inhibition of plant NRP1 and human SET/TAF-Iβ by cytochrome c during DNA damage response.

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Section: Resultssupporting

confidence: 93%

Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c

González‐Arzola

Díaz‐Quintana

Rivero-Rodríguez

et al. 2016

Nucleic Acids Research

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“…In addition, significant CSP are detected (Dd avg -P 0.05 ppm) for Lys7, Lys13, Val20, Ser47, Lys73, Val83, Lys88 and Ala92. Interestingly, Lys8, Lys13, Lys27, Lys72, Lys86 and Lys87 are all in contact with pCc 1 , as previously reported in chemical modification studies and molecular dynamics simulations [56][57][58]. When compared with pCc upon binding to pCc 1 [29], the map of CSP on the hCc surface differs at the level of those residues located far from the heme cleft.…”

Section: The Heterologous Hcc-pcc 1 Complexsupporting

confidence: 73%

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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“…3B)-thereby evidencing the key role of electrostatic forces in the formation of Cc:SET/TAF-Iβ complexes. Similarly, lysine residues are also involved in the interaction with cytochrome bc 1 (29,30). Given the well-known "lysine masking activity" of SET/TAF-Iβ that prevents the acetylation of histone lysines inside the INHAT complex (3), it is plausible that SET/TAF-Iβ also recognizes the lysine residues from Cc.…”

Section: Set/taf-iβ Histone-binding Domain Is Engaged During Binding 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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Mapping of the interaction domain for purified cytochrome c₁ on cytochrome c

Cited by 78 publications

References 13 publications

Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c

Histone chaperone activity of Arabidopsis thaliana NRP1 is blocked by cytochrome c

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

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