Search

Your search keyword '"Díaz-Quintana, Antonio"' showing total 23 results
Start Over Author "Díaz-Quintana, Antonio" Publisher wiley
23 results on '"Díaz-Quintana, Antonio"'

3. Proposed mechanism for regulation of H 2 O 2 ‐induced programmed cell death in plants by binding of cytochrome c to 14‐3‐3 proteins

Author

Elena‐Real, Carlos A., primary, González‐Arzola, Katiuska, additional, Pérez‐Mejías, Gonzalo, additional, Díaz‐Quintana, Antonio, additional, Velázquez‐Campoy, Adrián, additional, Desvoyes, Bénédicte, additional, Gutiérrez, Crisanto, additional, De la Rosa, Miguel A., additional, and Díaz‐Moreno, Irene, additional

Published
2021
Full Text
View/download PDF

7. Dimerization model of the C-terminal RNA Recognition Motif of HuR

Author

Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Junta de Andalucía, Díaz Quintana, Antonio Jesús, García Mauriño, Sofía M., Díaz Moreno, Irene, Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Junta de Andalucía, Díaz Quintana, Antonio Jesús, García Mauriño, Sofía M., and Díaz Moreno, Irene

Abstract

Human antigen R (HuR) is a ubiquitous 32kDa protein comprising three RNA Recognition Motifs (RRMs), whose main function is to bind Adenylate and uridylate Rich Elements (AREs) in 3′ UnTranslated Regions (UTRs) of mRNAs. In addition to binding RNA molecules, the third domain (RRM3) is involved in HuR oligomerization and apoptotic signaling. The RRM3 monomer is able to dimerize, with its self-binding affinity being dependent on ionic strength. Here we provide a deeper structural insight into the nature of the encounter complexes leading to the formation of RRM3 dimers by using Brownian Dynamics and Molecular Dynamics. Our computational data show that the initial unspecific encounter follows a downhill pathway until reaching an optimum conformation stabilized by hydrophobic interactions.

Published
2015

8. Mimicking Tyrosine Phosphorylation in Human Cytochrome cby the Evolved tRNA Synthetase Technique

Author

Guerra-Castellano, Alejandra, primary, Díaz-Quintana, Antonio, additional, Moreno-Beltrán, Blas, additional, López-Prados, Javier, additional, Nieto, Pedro M., additional, Meister, Wiebke, additional, Staffa, Jana, additional, Teixeira, Miguel, additional, Hildebrandt, Peter, additional, De la Rosa, Miguel A., additional, and Díaz-Moreno, Irene, additional

Published
2015
Full Text
View/download PDF

11. The cytochrome f–plastocyanin complex as a model to study transient interactions between redox proteins

Author

Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Ministerio de Ciencia e Innovación (MICIN). España, Junta de Andalucía, Cruz Gallardo, Isabel, Díaz Moreno, Irene, Díaz Quintana, Antonio Jesús, Rosa Acosta, Miguel Ángel de la, Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular, Ministerio de Ciencia e Innovación (MICIN). España, Junta de Andalucía, Cruz Gallardo, Isabel, Díaz Moreno, Irene, Díaz Quintana, Antonio Jesús, and Rosa Acosta, Miguel Ángel de la

Abstract

Transient complexes, with a lifetime ranging between microseconds and seconds, are essential forbiochemical reactions requiring a fast turnover. That is the case of the interactions between proteinsengaged in electron transfer reactions, which are involved in relevant physiological processes suchas respiration and photosynthesis. In the latter, the copper protein plastocyanin acts as a solublecarrier transferring electrons between the two membrane-embedded complexes cytochromeb6fand photosystem I. Here we review the combination of experimental efforts in the literature tounveil the functional and structural features of the complex between cytochromefand plastocya-nin, which have widely been used as a suitable model for analyzing transient redox interactions.

Published
2012

23. Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of Cytochrome c and Cardiolipin.

Author

Díaz-Quintana A, Pérez-Mejías G, Guerra-Castellano A, De la Rosa MA, and Díaz-Moreno I

Subjects
Humans, Models, Molecular, Cardiolipins metabolism, Cytochromes c metabolism, Mitochondrial Membranes metabolism
Abstract

Cardiolipin oxidation and degradation by different factors under severe cell stress serve as a trigger for genetically encoded cell death programs. In this context, the interplay between cardiolipin and another mitochondrial factor-cytochrome c -is a key process in the early stages of apoptosis, and it is a matter of intense research. Cytochrome c interacts with lipid membranes by electrostatic interactions, hydrogen bonds, and hydrophobic effects. Experimental conditions (including pH, lipid composition, and post-translational modifications) determine which specific amino acid residues are involved in the interaction and influence the heme iron coordination state. In fact, up to four binding sites (A, C, N, and L), driven by different interactions, have been reported. Nevertheless, key aspects of the mechanism for cardiolipin oxidation by the hemeprotein are well established. First, cytochrome c acts as a pseudoperoxidase, a process orchestrated by tyrosine residues which are crucial for peroxygenase activity and sensitivity towards oxidation caused by protein self-degradation. Second, flexibility of two weakest folding units of the hemeprotein correlates with its peroxidase activity and the stability of the iron coordination sphere. Third, the diversity of the mode of interaction parallels a broad diversity in the specific reaction pathway. Thus, current knowledge has already enabled the design of novel drugs designed to successfully inhibit cardiolipin oxidation., Competing Interests: The authors declare that there is no conflict of interest regarding the publication of this review article., (Copyright © 2020 Antonio Díaz-Quintana et al.)

Published
2020
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results