scholarly journals Charge Interactions Modulate the Encounter Complex Ensemble of Two Differently Charged Disordered Protein Partners of KIX

2020 ◽  
Vol 16 (6) ◽  
pp. 3856-3868 ◽  
Author(s):  
Wen-Ting Chu ◽  
Sarah L. Shammas ◽  
Jin Wang
Keyword(s):  
Disordered Protein ◽  
Protein Partners ◽  
Encounter Complex ◽  
Charge Interactions

scholarly journals Pneumoviral Phosphoprotein, a Multidomain Adaptor-Like Protein of Apparent Low Structural Complexity and High Conformational Versatility

2021 ◽  
Vol 22 (4) ◽  
pp. 1537
Author(s):  
Christophe Cardone ◽  
Claire-Marie Caseau ◽  
Nelson Pereira ◽  
Christina Sizun
Keyword(s):  
3D Structure ◽  
Structural Complexity ◽  
Intrinsically Disordered Protein ◽  
Structural Features ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Disordered Protein ◽  
Protein Partners ◽  
P Proteins ◽  
Oligomerization Domain

Mononegavirales phosphoproteins (P) are essential co-factors of the viral polymerase by serving as a linchpin between the catalytic subunit and the ribonucleoprotein template. They have highly diverged, but their overall architecture is conserved. They are multidomain proteins, which all possess an oligomerization domain that separates N- and C-terminal domains. Large intrinsically disordered regions constitute their hallmark. Here, we exemplify their structural features and interaction potential, based on the Pneumoviridae P proteins. These P proteins are rather small, and their oligomerization domain is the only part with a defined 3D structure, owing to a quaternary arrangement. All other parts are either flexible or form short-lived secondary structure elements that transiently associate with the rest of the protein. Pneumoviridae P proteins interact with several viral and cellular proteins that are essential for viral transcription and replication. The combination of intrinsic disorder and tetrameric organization enables them to structurally adapt to different partners and to act as adaptor-like platforms to bring the latter close in space. Transient structures are stabilized in complex with protein partners. This class of proteins gives an insight into the structural versatility of non-globular intrinsically disordered protein domains.

scholarly journals The Unconventional Self-Cleavage of Selenoprotein K

2021 ◽  
Author(s):  
Rujin Cheng ◽  
Jun Liu ◽  
Martin Forstner ◽  
George Woodward ◽  
Elmer Heppard ◽  
...  
Keyword(s):  
Intrinsically Disordered Protein ◽  
Cellular Functions ◽  
Peptide Bonds ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Catalytic Function ◽  
Protein Partners ◽  
Selenoprotein K

Through known association with other proteins, human selenoprotein K (selenok) is currently implicated in the palmitoylation of proteins, degradation of misfolded proteins, innate immune response, and the life cycle of SARS-CoV-2 virus. However, neither the catalytic function of selenok's selenocysteine (Sec), which, curiously, resides in an intrinsically disordered protein segment nor selenok's specific role in these pathways are known to date. This report casts these questions in a new light as it describes that selenok is able -both in vitro and in vivo- to cleave some of its own peptide bonds. The cleavages not only release selenok segments that contain its reactive Sec, but as the specific cleavage sites were identified, they proved to cluster tightly near sites through which selenok interacts with protein partners. Furthermore, it is shown that selenok's cleavage activity is neither restricted to itself nor promiscuous but selectively extends to at least one of its protein partners. Together, selenok's cleavage ability and its features have all hallmarks of a regulatory mechanism that could play a central role in selenok's associations with other proteins and its cellular functions overall.

scholarly journals The interactome of multifunctional HAX1 protein suggests its role in the regulation of energy metabolism, de-aggregation, cytoskeleton organization and RNA-processing

2020 ◽  
Vol 40 (11) ◽  
Author(s):  
Maciej Wakula ◽  
Anna Balcerak ◽  
Tymon Rubel ◽  
Mateusz Chmielarczyk ◽  
Ryszard Konopinski ◽  
...  
Keyword(s):  
Cellular Response ◽  
Wide Spectrum ◽  
Intrinsically Disordered Protein ◽  
Multifunctional Protein ◽  
Cytoskeleton Organization ◽  
Cellular Processes ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Protein Partners ◽  
Protein Interactome

Abstract HCLS1-associated protein X-1 (HAX1) is a multifunctional protein involved in many cellular processes, including apoptosis, cell migration and calcium homeostasis, but its mode of action still remains obscure. Multiple HAX1 protein partners have been identified, but they are involved in many distinct pathways, form different complexes and do not constitute a coherent group. By characterizing HAX1 protein interactome using targeted approach, we attempt to explain HAX1 multiple functions and its role in the cell. Presented analyses indicate that HAX1 interacts weakly with a wide spectrum of proteins and its interactome tends to be cell-specific, which conforms to a profile of intrinsically disordered protein (IDP). Moreover, we have identified a mitochondrial subset of HAX1 protein partners and preliminarily characterized its involvement in the cellular response to oxidative stress and aggregation.

Direct Molecular Fishing of New Protein Partners for Human Thromboxane Synthase

Acta Naturae ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 92-100 ◽  
Author(s):  
A. V. Svirid ◽  
◽  
P. V. Ershov ◽  
E. O. Yablokov ◽  
L. A. Kaluzhskiy ◽  
...  
Keyword(s):  
Thromboxane Synthase ◽  
Protein Partners ◽  
Molecular Fishing ◽  
New Protein

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

2018 ◽  
Author(s):  
Sarah Klass ◽  
Matthew J. Smith ◽  
Tahoe Fiala ◽  
Jessica Lee ◽  
Anthony Omole ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Fusion Proteins ◽  
Organic Molecules ◽  
Intrinsically Disordered Protein ◽  
Protein Domain ◽  
Enzymatic Cleavage ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Self Assembling ◽  
Protein Tag

Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on a human intrinsically disordered protein, which has been appended with a hydrophobic segment. The micelles were found to form across a broad range of pH, ionic strength, and temperature conditions, with critical micelle concentration (CMC) values below 1 µM being observed in some cases. The reported micelles were found to solubilize hydrophobic metal complexes and organic molecules, suggesting their potential suitability for catalysis and drug delivery applications.

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