Clusters in an Intrinsically Disordered Protein Create a Protein-Binding Site:  The TolB-Binding Region of Colicin E9†

Biochemistry ◽  
2005 ◽  
Vol 44 (34) ◽  
pp. 11496-11507 ◽  
Author(s):  
Kaeko Tozawa ◽  
Colin J. Macdonald ◽  
Christopher N. Penfold ◽  
Richard James ◽  
Colin Kleanthous ◽  
...  
Keyword(s):  
Protein Binding ◽  
Binding Site ◽  
Intrinsically Disordered Protein ◽  
Protein Binding Site ◽  
Binding Region ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Colicin E9

scholarly journals Intrinsically Disordered Protein Threads Through the Bacterial Outer-Membrane Porin OmpF

Science ◽  
2013 ◽  
Vol 340 (6140) ◽  
pp. 1570-1574 ◽  
Author(s):  
Nicholas G. Housden ◽  
Jonathan T. S. Hopper ◽  
Natalya Lukoyanova ◽  
David Rodriguez-Larrea ◽  
Justyna A. Wojdyla ◽  
...  
Keyword(s):  
Cell Death ◽  
Outer Membrane ◽  
Outer Membrane Proteins ◽  
Intrinsically Disordered Protein ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Outer Membrane Porin ◽  
Fixed Orientation ◽  
Bacterial Outer Membrane ◽  
Colicin E9

Porins are β-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9’s unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membrane in a fixed orientation that triggers colicin import. Thus, an intrinsically disordered protein can tunnel through the narrow pores of an oligomeric porin to deliver an epitope signal to the cell to initiate cell death.

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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