The role of proteomics in studies of protein moonlighting

2014 ◽  
Vol 42 (6) ◽  
pp. 1698-1703 ◽  
Author(s):  
Robert J. Beynon ◽  
Dean Hammond ◽  
Victoria Harman ◽  
Yvonne Woolerton
Keyword(s):  
Post Translational Modifications ◽  
Multiple Functions ◽  
Protein Mixture ◽  
Complex Protein Mixture ◽  
Complex Protein ◽  
Quantitative Approaches

The increasing acceptance that proteins may exert multiple functions in the cell brings with it new analytical challenges that will have an impact on the field of proteomics. Many proteomics workflows begin by destroying information about the interactions between different proteins, and the reduction of a complex protein mixture to constituent peptides also scrambles information about the combinatorial potential of post-translational modifications. To bring the focus of proteomics on to the domain of protein moonlighting will require novel analytical and quantitative approaches.

Fractionation of Complex Protein Mixture by Virtual Three-Dimensional Liquid Chromatography Based on Combined pH and Salt Steps

2008 ◽  
Vol 7 (10) ◽  
pp. 4525-4537 ◽  
Author(s):  
Zhi-Bin Ning ◽  
Qing-Run Li ◽  
Jie Dai ◽  
Rong-Xia Li ◽  
Chia-Hui Shieh ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Three Dimensional ◽  
Protein Mixture ◽  
Complex Protein Mixture ◽  
Complex Protein

Development of Ubiquitin Tools for Studies of Complex Ubiquitin Processing Protein Machines

2020 ◽  
Vol 23 (23) ◽  
pp. 2614-2625
Author(s):  
Xin Sui ◽  
Yi-Ming Li
Keyword(s):  
Protein Localization ◽  
The Other ◽  
Related Protein ◽  
Deubiquitinating Enzymes ◽  
Post Translational Modifications ◽  
Physiological Processes ◽  
Complex Protein ◽  
Recombinant Technology ◽  
Functional Mechanisms

: Ubiquitination is one of the most extensive post-translational modifications in eukaryotes and is involved in various physiological processes such as protein degradation, autophagy, protein interaction, and protein localization. The ubiquitin (Ub)-related protein machines include Ub-activating enzymes (E1s), Ub-conjugating enzymes (E2s), Ub ligases (E3s), deubiquitinating enzymes (DUBs), p97, and the proteasomes. In recent years, the role of DUBs has been extensively studied and relatively well understood. On the other hand, the functional mechanisms of the other more complex ubiquitin-processing protein machines (e.g., E3, p97, and proteasomes) are still to be sufficiently well explored due to their intricate nature. One of the hurdles facing the studies of these complex protein machines is the challenge of developing tailor-designed structurally defined model substrates, which unfortunately cannot be directly obtained using recombinant technology. Consequently, the acquisition and synthesis of the ubiquitin tool molecules are essential for the elucidation of the functions and structures of the complex ubiquitin-processing protein machines. This paper aims to highlight recent studies on these protein machines based on the synthetic ubiquitin tool molecules.

Unravelling Nonspecific Adsorption of Complex Protein Mixture on Surfaces with SPR and MS

2014 ◽  
Vol 86 (19) ◽  
pp. 9612-9619 ◽  
Author(s):  
Julien Breault-Turcot ◽  
Pierre Chaurand ◽  
Jean-Francois Masson
Keyword(s):  
Nonspecific Adsorption ◽  
Protein Mixture ◽  
Complex Protein Mixture ◽  
Complex Protein

Matrigel: A complex protein mixture required for optimal growth of cell culture

PROTEOMICS ◽  
2010 ◽  
Vol 10 (9) ◽  
pp. 1886-1890 ◽  
Author(s):  
Chris S. Hughes ◽  
Lynne M. Postovit ◽  
Gilles A. Lajoie
Keyword(s):  
Cell Culture ◽  
Optimal Growth ◽  
Protein Mixture ◽  
Complex Protein Mixture ◽  
Complex Protein

Comparison of displacement versus gradient mode for separation of a complex protein mixture by anion-exchange chromatography

2012 ◽  
Vol 901 ◽  
pp. 34-40 ◽  
Author(s):  
Robert Ahrends ◽  
Björn Lichtner ◽  
Friedrich Buck ◽  
Diana Hildebrand ◽  
Marta Kotasinska ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Protein Mixture ◽  
Complex Protein Mixture ◽  
Complex Protein ◽  
Gradient Mode

scholarly journals Mechanism of the small ATP-independent chaperone Spy is substrate specific

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Rishav Mitra ◽  
Varun V. Gadkari ◽  
Ben A. Meinen ◽  
Carlo P. M. van Mierlo ◽  
Brandon T. Ruotolo ◽  
...  
Keyword(s):  
Relative Affinity ◽  
Complex Protein ◽  
Partially Unfolded ◽  
Substrate Proteins ◽  
Partially Unfolded States

AbstractATP-independent chaperones are usually considered to be holdases that rapidly bind to non-native states of substrate proteins and prevent their aggregation. These chaperones are thought to release their substrate proteins prior to their folding. Spy is an ATP-independent chaperone that acts as an aggregation inhibiting holdase but does so by allowing its substrate proteins to fold while they remain continuously chaperone bound, thus acting as a foldase as well. The attributes that allow such dual chaperoning behavior are unclear. Here, we used the topologically complex protein apoflavodoxin to show that the outcome of Spy’s action is substrate specific and depends on its relative affinity for different folding states. Tighter binding of Spy to partially unfolded states of apoflavodoxin limits the possibility of folding while bound, converting Spy to a holdase chaperone. Our results highlight the central role of the substrate in determining the mechanism of chaperone action.

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