scholarly journals A molecular recognition feature mediates ribosome-induced SRP-receptor assembly during protein targeting

2019 ◽  
Vol 218 (10) ◽  
pp. 3307-3319 ◽  
Author(s):  
Yu-Hsien Hwang Fu ◽  
Sowmya Chandrasekar ◽  
Jae Ho Lee ◽  
Shu-ou Shan
Keyword(s):  
Molecular Recognition ◽  
Protein Targeting ◽  
Signal Recognition Particle ◽  
Intrinsically Disordered Protein ◽  
Signal Recognition ◽  
Cellular Functions ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Linker Domain ◽  
Receptor Assembly

Molecular recognition features (MoRFs) provide interaction motifs in intrinsically disordered protein regions to mediate diverse cellular functions. Here we report that a MoRF element, located in the disordered linker domain of the mammalian signal recognition particle (SRP) receptor and conserved among eukaryotes, plays an essential role in sensing the ribosome during cotranslational protein targeting to the endoplasmic reticulum. Loss of the MoRF in the SRP receptor (SR) largely abolishes the ability of the ribosome to activate SRP-SR assembly and impairs cotranslational protein targeting. These results demonstrate a novel role for MoRF elements and provide a mechanism for the ribosome-induced activation of the mammalian SRP pathway. Kinetic analyses and comparison with the bacterial SRP further suggest that the SR MoRF functionally replaces the essential GNRA tetraloop in the bacterial SRP RNA, providing an example for the replacement of RNA function by proteins during the evolution of ancient ribonucleoprotein particles.

scholarly journals Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Angelo Toto ◽  
Carlo Camilloni ◽  
Rajanish Giri ◽  
Maurizio Brunori ◽  
Michele Vendruscolo ◽  
...  
Keyword(s):  
Molecular Recognition ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein

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 Molecular recognition features (MoRFs) in three domains of life

2016 ◽  
Vol 12 (3) ◽  
pp. 697-710 ◽  
Author(s):  
Jing Yan ◽  
A. Keith Dunker ◽  
Vladimir N. Uversky ◽  
Lukasz Kurgan
Keyword(s):  
Amino Acid ◽  
Molecular Recognition ◽  
Protein Binding ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Domains Of Life ◽  
Molecular Recognition Features

MoRFs are widespread intrinsically disordered protein-binding regions that have similar abundance and amino acid composition across the three domains of life.

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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