Flavodoxin-Mediated Electron Transfer from Photosystem I to Ferredoxin-NADP+Reductase inAnabaena:  Role of Flavodoxin Hydrophobic Residues in Protein−Protein Interactions†

Biochemistry ◽  
2008 ◽  
Vol 47 (4) ◽  
pp. 1207-1217 ◽  
Author(s):  
Guillermina Goñi ◽  
Ana Serrano ◽  
Susana Frago ◽  
Manuel Hervás ◽  
José Ramón Peregrina ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photosystem I ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Hydrophobic Residues ◽  
Mediated Electron Transfer

Role of Hydrophobic Interactions in the Flavodoxin Mediated Electron Transfer from Photosystem I to Ferredoxin-NADP+Reductase inAnabaenaPCC 7119†

Biochemistry ◽  
2003 ◽  
Vol 42 (7) ◽  
pp. 2036-2045 ◽  
Author(s):  
Isabel Nogués ◽  
Marta Martínez-Júlvez ◽  
José A. Navarro ◽  
Manuel Hervás ◽  
Lorena Armenteros ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Photosystem I ◽  
Hydrophobic Interactions ◽  
Mediated Electron Transfer

scholarly journals Customized exogenous ferredoxin functions as an efficient electron carrier

2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Zhan Song ◽  
Cancan Wei ◽  
Chao Li ◽  
Xin Gao ◽  
Shuhong Mao ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Protein Interactions ◽  
Reaction System ◽  
Protein Protein Interactions ◽  
Electron Transfer Process ◽  
Potential Measurement ◽  
Electron Carrier ◽  
Electron Transfer Pathway ◽  
Biological Electron Transfer

AbstractFerredoxin (Fdx) is regarded as the main electron carrier in biological electron transfer and acts as an electron donor in metabolic pathways of many organisms. Here, we screened a self-sufficient P450-derived reductase PRF with promising production yield of 9OHAD (9α-hydroxy4-androstene-3,17-dione) from AD, and further proved the importance of [2Fe–2S] clusters of ferredoxin-oxidoreductase in transferring electrons in steroidal conversion. The results of truncated Fdx domain in all oxidoreductases and mutagenesis data elucidated the indispensable role of [2Fe–2S] clusters in the electron transfer process. By adding the independent plant-type Fdx to the reaction system, the AD (4-androstene-3,17-dione) conversion rate have been significantly improved. A novel efficient electron transfer pathway of PRF + Fdx + KshA (KshA, Rieske-type oxygenase of 3-ketosteroid-9-hydroxylase) in the reaction system rather than KshAB complex system was proposed based on analysis of protein–protein interactions and redox potential measurement. Adding free Fdx created a new conduit for electrons to travel from reductase to oxygenase. This electron transfer pathway provides new insight for the development of efficient exogenous Fdx as an electron carrier. Graphical Abstract

scholarly journals Customized exogenous ferredoxin functions as an efficient electron carrier

2021 ◽  
Author(s):  
Zhan Song ◽  
Cancan Wei ◽  
Chao Li ◽  
Xin Gao ◽  
Shuhong Mao ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Protein Interactions ◽  
Reaction System ◽  
Protein Protein Interactions ◽  
Potential Measurement ◽  
Electron Carrier ◽  
Electron Transfer Pathway ◽  
Reduction Activity ◽  
Biological Electron Transfer

Ferredoxin (Fdx) is regarded as the main electron carrier in biological electron transfer and acts as an electron donor in metabolic pathways of many organisms. Here, we screened a self-sufficient P450-derived reductase PRF with promising NADPH reduction activity and 9OHAD production yield and proved the importance of [2Fe-2S] clusters of Fdx-containing oxidoreductase in transferring electrons in steroidal conversion. The truncated Fdx domain in all oxidoreductases, together with mutagenesis data, further elucidated the indispensable role of [2Fe-2S] clusters in the electron transfer process. By adding the independent plant-type Fdx to the reaction system, the AD conversion rate have been significantly improved. A novel efficient electron transfer pathway of PRF+Fdx+KshA in the reaction system rather than KshAB complex system was proposed based on analysis of protein-protein interactions and redox potential measurement. Adding free Fdx created a new conduit for electrons to travel from reductase to oxygenase. This electron transfer pathway provides new insight for the development of efficient exogenous Fdx as an electron carrier.

scholarly journals Photosynthetic Electron Transfer by Dint of Protein Mobile Carriers. Multi-particle Brownian and Molecular Modeling

2019 ◽  
Vol 224 ◽  
pp. 03008
Author(s):  
Galina Riznichenk ◽  
Ilya Kovalenko ◽  
Vladimir Fedorov ◽  
Sergei Khruschev ◽  
Andrey Rubin
Keyword(s):  
Electron Transfer ◽  
Photosystem I ◽  
Protein Interactions ◽  
Thylakoid Membrane ◽  
Electrostatic Interactions ◽  
Simulation Method ◽  
Photosynthetic Membrane ◽  
Dynamic Simulations ◽  
Multienzyme Complexes

The paper presents the review of works on modeling the interaction of photosynthetic proteins using the multiparticle Brownian dynamics method developed at the Department of Biophysics, Biological Faculty, Lomonosov Moscow State University. The method describes the displacement of individual macromolecules – mobile electron carriers, and their electrostatic interactions between each other and with pigment-protein complexes embedded in photosynthetic membrane. Three-dimensional models of the protein molecules were constructed on the basis of the data from the Protein Data Bank. We applied the Brownian methods coupled to molecular dynamic simulations to reveal the role of electrostatic interactions and conformational motions in the transfer of an electron from the cytochrome complex Cyt b6f) membrane we developed the model which combines events of proteins Pc diffusion along the thylakoid membrane, electrostatic interactions of Pc with the membrane charges, formation of Pc super-complexes with multienzyme complexes of Photosystem I and to the molecule of the mobile carrier plastocyanin (Pc) in plants, green algae and cyanic bacteria. Taking into account the interior of photosynthetic membrane we developed the model which combines events of proteins Pc diffusion along the thylakoid membrane, electrostatic interactions of Pc with the membrane charges, formation of Pc super-complexes with multienzyme complexes of Photosystem I and Cyt b6f, embedded in photosynthetic membrane, electron transfer and complex dissociation. Multiparticle Brownian simulation method can be used to consider the processes of protein interactions in subcellular systems in order to clarify the role of individual stages and the biophysical mechanisms of these processes.

scholarly journals Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein

2021 ◽  
Vol 43 (2) ◽  
pp. 767-781
Author(s):  
Vanessa Pinatto Gaspar ◽  
Anelise Cardoso Ramos ◽  
Philippe Cloutier ◽  
José Renato Pattaro Junior ◽  
Francisco Ferreira Duarte Junior ◽  
...  
Keyword(s):  
Dna Replication ◽  
Protein Interactions ◽  
Ribosome Biogenesis ◽  
Cell Metabolism ◽  
Cell Types ◽  
Protein Protein Interactions ◽  
Cellular Mechanisms ◽  
Cancerous Cell ◽  
First Time

KIN (Kin17) protein is overexpressed in a number of cancerous cell lines, and is therefore considered a possible cancer biomarker. It is a well-conserved protein across eukaryotes and is ubiquitously expressed in all cell types studied, suggesting an important role in the maintenance of basic cellular function which is yet to be well determined. Early studies on KIN suggested that this nuclear protein plays a role in cellular mechanisms such as DNA replication and/or repair; however, its association with chromatin depends on its methylation state. In order to provide a better understanding of the cellular role of this protein, we investigated its interactome by proximity-dependent biotin identification coupled to mass spectrometry (BioID-MS), used for identification of protein–protein interactions. Our analyses detected interaction with a novel set of proteins and reinforced previous observations linking KIN to factors involved in RNA processing, notably pre-mRNA splicing and ribosome biogenesis. However, little evidence supports that this protein is directly coupled to DNA replication and/or repair processes, as previously suggested. Furthermore, a novel interaction was observed with PRMT7 (protein arginine methyltransferase 7) and we demonstrated that KIN is modified by this enzyme. This interactome analysis indicates that KIN is associated with several cell metabolism functions, and shows for the first time an association with ribosome biogenesis, suggesting that KIN is likely a moonlight protein.

scholarly journals On the role of non-diagonal system–environment interactions in bridge-mediated electron transfer

2020 ◽  
Vol 153 (18) ◽  
pp. 185101
Author(s):  
Nirmalendu Acharyya ◽  
Roman Ovcharenko ◽  
Benjamin P. Fingerhut
Keyword(s):  
Electron Transfer ◽  
System Environment ◽  
Diagonal System ◽  
Mediated Electron Transfer

Structure, Function, Involvement in Diseases and Targeting of 14-3-3 Proteins: An Update

2018 ◽  
Vol 25 (1) ◽  
pp. 5-21 ◽  
Author(s):  
Ylenia Cau ◽  
Daniela Valensin ◽  
Mattia Mori ◽  
Sara Draghi ◽  
Maurizio Botta
Keyword(s):  
Protein Interactions ◽  
Molecular Mechanisms ◽  
Physiological Role ◽  
Specific Protein ◽  
Protein Protein Interactions ◽  
Cellular Processes ◽  
Protein Partners ◽  
High Sequence Homology ◽  
Small Molecule Modulators

14-3-3 is a class of proteins able to interact with a multitude of targets by establishing protein-protein interactions (PPIs). They are usually found in all eukaryotes with a conserved secondary structure and high sequence homology among species. 14-3-3 proteins are involved in many physiological and pathological cellular processes either by triggering or interfering with the activity of specific protein partners. In the last years, the scientific community has collected many evidences on the role played by seven human 14-3-3 isoforms in cancer or neurodegenerative diseases. Indeed, these proteins regulate the molecular mechanisms associated to these diseases by interacting with (i) oncogenic and (ii) pro-apoptotic proteins and (iii) with proteins involved in Parkinson and Alzheimer diseases. The discovery of small molecule modulators of 14-3-3 PPIs could facilitate complete understanding of the physiological role of these proteins, and might offer valuable therapeutic approaches for these critical pathological states.

scholarly journals Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions

2016 ◽  
Vol 3 ◽  
Author(s):  
Elise Delaforge ◽  
Sigrid Milles ◽  
Jie-rong Huang ◽  
Denis Bouvier ◽  
Malene Ringkjøbing Jensen ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Large Scale ◽  
Protein Protein Interactions ◽  
Domain Dynamics

scholarly journals The Role of Posttranslational Modifications in DNA Repair

2020 ◽  
Vol 2020 ◽  
pp. 1-13
Author(s):  
Miaomiao Bai ◽  
Dongdong Ti ◽  
Qian Mei ◽  
Jiejie Liu ◽  
Xin Yan ◽  
...  
Keyword(s):  
Dna Damage ◽  
Dna Repair ◽  
Protein Interactions ◽  
Posttranslational Modifications ◽  
Genome Stability ◽  
Protein Localization ◽  
Complex Structure ◽  
Protein Protein Interactions ◽  
Regulate Protein

The human body is a complex structure of cells, which are exposed to many types of stress. Cells must utilize various mechanisms to protect their DNA from damage caused by metabolic and external sources to maintain genomic integrity and homeostasis and to prevent the development of cancer. DNA damage inevitably occurs regardless of physiological or abnormal conditions. In response to DNA damage, signaling pathways are activated to repair the damaged DNA or to induce cell apoptosis. During the process, posttranslational modifications (PTMs) can be used to modulate enzymatic activities and regulate protein stability, protein localization, and protein-protein interactions. Thus, PTMs in DNA repair should be studied. In this review, we will focus on the current understanding of the phosphorylation, poly(ADP-ribosyl)ation, ubiquitination, SUMOylation, acetylation, and methylation of six typical PTMs and summarize PTMs of the key proteins in DNA repair, providing important insight into the role of PTMs in the maintenance of genome stability and contributing to reveal new and selective therapeutic approaches to target cancers.

scholarly journals Bi-directional protein-protein interactions control liquid-liquid phase separation of PSD-95 and its interaction partners

2021 ◽  
Author(s):  
Nikolaj Riis Christensen ◽  
Christian Parsbæk Pedersen ◽  
Vita Sereikaite ◽  
Jannik Nedergaard Pedersen ◽  
Maria Vistrup-Parry ◽  
...  
Keyword(s):  
Phase Separation ◽  
Liquid Phase ◽  
Protein Interactions ◽  
Postsynaptic Density ◽  
Specific Protein ◽  
Liquid Phase Separation ◽  
Protein Protein Interactions ◽  
New Perspective ◽  
Liquid Liquid Phase Separation

SUMMARYThe organization of the postsynaptic density (PSD), a protein-dense semi-membraneless organelle, is mediated by numerous specific protein-protein interactions (PPIs) which constitute a functional post-synapse. Postsynaptic density protein 95 (PSD-95) interacts with a manifold of proteins, including the C-terminal of transmembrane AMPA receptor (AMAPR) regulatory proteins (TARPs). Here, we uncover the minimal essential peptide responsible for the stargazin (TARP-γ2) mediated liquid-liquid phase separation (LLPS) formation of PSD-95 and other key protein constituents of the PSD. Furthermore, we find that pharmacological inhibitors of PSD-95 can facilitate formation of LLPS. We found that in some cases LLPS formation is dependent on multivalent interactions while in other cases short peptides carrying a high charge are sufficient to promote LLPS in complex systems. This study offers a new perspective on PSD-95 interactions and their role in LLPS formation, while also considering the role of affinity over multivalency in LLPS systems.

Sign in / Sign up

Export Citation Format

Share Document