scholarly journals Sulfation, the Up-and-Coming Post-Translational Modification:  Its Role and Mechanism in Protein−Protein Interaction

2007 ◽  
Vol 6 (3) ◽  
pp. 1176-1182 ◽  
Author(s):  
Amina S. Woods ◽  
Hay-Yan J. Wang ◽  
Shelley N. Jackson
Keyword(s):  
Protein Interaction ◽  
Post Translational Modification ◽  
Protein Protein Interaction

scholarly journals Protein-protein-interaction Network Organization of the Hypusine Modification System

2012 ◽  
Vol 11 (11) ◽  
pp. 1289-1305 ◽  
Author(s):  
Henning Sievert ◽  
Simone Venz ◽  
Oscar Platas-Barradas ◽  
Vishnu M. Dhople ◽  
Martin Schaletzky ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Large Scale ◽  
Affinity Purification ◽  
Interaction Network ◽  
Initiation Factor ◽  
Post Translational Modification ◽  
Comprehensive Overview ◽  
Data Set ◽  
Modification System ◽  
Protein Protein Interaction

Hypusine modification of eukaryotic initiation factor 5A (eIF-5A) represents a unique and highly specific post-translational modification with regulatory functions in cancer, diabetes, and infectious diseases. However, the specific cellular pathways that are influenced by the hypusine modification remain largely unknown. To globally characterize eIF-5A and hypusine-dependent pathways, we used an approach that combines large-scale bioreactor cell culture with tandem affinity purification and mass spectrometry: “bioreactor-TAP-MS/MS.” By applying this approach systematically to all four components of the hypusine modification system (eIF-5A1, eIF-5A2, DHS, and DOHH), we identified 248 interacting proteins as components of the cellular hypusine network, with diverse functions including regulation of translation, mRNA processing, DNA replication, and cell cycle regulation. Network analysis of this data set enabled us to provide a comprehensive overview of the protein-protein interaction landscape of the hypusine modification system. In addition, we validated the interaction of eIF-5A with some of the newly identified associated proteins in more detail. Our analysis has revealed numerous novel interactions, and thus provides a valuable resource for understanding how this crucial homeostatic signaling pathway affects different cellular functions.

Envisioning the immune interactome in Arabidopsis

2020 ◽  
Vol 47 (6) ◽  
pp. 486
Author(s):  
Rashmi Maurya ◽  
Deepti Srivastava ◽  
Munna Singh ◽  
Samir V. Sawant
Keyword(s):  
Protein Interaction ◽  
Plant Pathogen ◽  
Post Translational Modification ◽  
Kinase Substrate ◽  
Protein Protein Interaction ◽  
Signal Perception ◽  
Substrate Protein ◽  
Molecular Machinery ◽  
Plant Pathogen Interaction ◽  
Plant Pathogenesis

During plant–pathogen interaction, immune targets were regulated by protein–protein interaction events such as ligand-receptor/co-receptor, kinase-substrate, protein sequestration, activation or repression via post-translational modification and homo/oligo/hetro-dimerisation of proteins. A judicious use of molecular machinery requires coordinated protein interaction among defence components. Immune signalling in Arabidopsis can be broadly represented in successive or simultaneous steps; pathogen recognition at cell surface, Ca2+ and reactive oxygen species signalling, MAPK signalling, post-translational modification, transcriptional regulation and phyto-hormone signalling. Proteome wide interaction studies have shown the existence of interaction hubs associated with physiological function. So far, a number of protein interaction events regulating immune targets have been identified, but their understanding in an interactome view is lacking. We focussed specifically on the integration of protein interaction signalling in context to plant–pathogenesis and identified the key targets. The present review focuses towards a comprehensive view of the plant immune interactome including signal perception, progression, integration and physiological response during plant pathogen interaction.

scholarly journals MetOSite: an integrated resource for the study of methionine residues sulfoxidation

2019 ◽  
Vol 35 (22) ◽  
pp. 4849-4850 ◽  
Author(s):  
Héctor Valverde ◽  
Francisco R Cantón ◽  
Juan Carlos Aledo
Keyword(s):  
Protein Interaction ◽  
Protein Function ◽  
Redox Regulation ◽  
Homo Sapiens ◽  
Methionine Sulfoxide ◽  
Subcellular Location ◽  
Biological Properties ◽  
Post Translational Modification ◽  
Protein Protein Interaction ◽  
Methionine Residues

Abstract Motivation The oxidation of protein-bound methionine to form methionine sulfoxide has traditionally been regarded as an oxidative damage. However, growing evidences support the view of this reversible reaction also as a regulatory post-translational modification. Thus, the oxidation of methionine residues has been reported to have multiple and varied implications for protein function. However, despite the importance of this modification and the abundance of reports, all these data are scattered in the literature. No database/resource on methionine sulfoxidation exists currently. Since this information is useful to gain further insights into the redox regulation of cellular proteins, we have created a primary database of experimentally confirmed sulfoxidation sites. Results MetOSite currently contains 7242 methionine sulfoxide sites found in 3562 different proteins from 23 species, with Homo sapiens, Arabidopsis thaliana and Bacillus cereus as the main contributors. Each collected site has been classified according to the effect of its sulfoxidation on the biological properties of the modified protein. Thus, MetOSite documents cases where the sulfoxidation of methionine leads to (i) gain of activity, (ii) loss of activity, (iii) increased protein–protein interaction susceptibility, (iv) decreased protein–protein interaction susceptibility, (v) changes in protein stability and (vi) changes in subcellular location. Availability and implementation MetOSite is available at https://metosite.uma.es.

An efficient transient assays system using Agrobacterium-mediated transformation of onion (Allium cepa) epidermal cells

2020 ◽  
Vol 80 (03) ◽  
Author(s):  
Yu-Miao Zhang ◽  
Jun Wang ◽  
Tao Wu
Keyword(s):  
Subcellular Localization ◽  
Protein Interaction ◽  
Protein Interactions ◽  
Epidermal Cells ◽  
Cyclin Dependent Kinase ◽  
Protein Subcellular Localization ◽  
Protein Protein Interactions ◽  
Efficient System ◽  
Protein Protein Interaction ◽  
Onion Epidermal Cells

In this study, the Agrobacterium infection medium, infection duration, detergent, and cell density were optimized. The sorghum-based infection medium (SbIM), 10-20 min infection time, addition of 0.01% Silwet L-77, and Agrobacterium optical density at 600 nm (OD600), improved the competence of onion epidermal cells to support Agrobacterium infection at >90% efficiency. Cyclin-dependent kinase D-2 (CDKD-2) and cytochrome c-type biogenesis protein (CYCH), protein-protein interactions were localized. The optimized procedure is a quick and efficient system for examining protein subcellular localization and protein-protein interaction.

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