Verification of the Stabilized Protein Design Based on the Prediction of Intrinsically Disordered Regions: Ribosomal Proteins L1

2020 ◽  
Vol 85 (1) ◽  
pp. 90-98
Author(s):  
G. S. Nagibina ◽  
V. V. Marchenkov ◽  
K. A. Glukhova ◽  
T. N. Melnik ◽  
B. S. Melnik
Keyword(s):  
Protein Design ◽  
Ribosomal Proteins ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Disordered Regions

scholarly journals Tsr4 Is a Cytoplasmic Chaperone for the Ribosomal Protein Rps2 in Saccharomyces cerevisiae

2019 ◽  
Vol 39 (17) ◽  
Author(s):  
Joshua J. Black ◽  
Sharmishtha Musalgaonkar ◽  
Arlen W. Johnson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Unknown Function ◽  
Ribosomal Proteins ◽  
Ribosome Biogenesis ◽  
Eukaryotic Ribosome ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Nonspecific Interactions ◽  
Disordered Regions

ABSTRACT Eukaryotic ribosome biogenesis requires the action of approximately 200 trans-acting factors and the incorporation of 79 ribosomal proteins (RPs). The delivery of RPs to preribosomes is a major challenge for the cell because RPs are often highly basic and contain intrinsically disordered regions prone to nonspecific interactions and aggregation. To counteract this, eukaryotes developed dedicated chaperones for certain RPs that promote their solubility and expression, often by binding eukaryote-specific extensions of the RPs. Rps2 (uS5) is a universally conserved RP that assembles into nuclear pre-40S subunits. However, a chaperone for Rps2 had not been identified. Our laboratory previously characterized Tsr4 as a 40S biogenesis factor of unknown function. Here, we report that Tsr4 cotranslationally associates with Rps2. Rps2 harbors a eukaryote-specific N-terminal extension that is critical for its interaction with Tsr4. Moreover, Tsr4 perturbation resulted in decreased Rps2 levels and phenocopied Rps2 depletion. Despite Rps2 joining nuclear pre-40S particles, Tsr4 appears to be restricted to the cytoplasm. Thus, we conclude that Tsr4 is a cytoplasmic chaperone dedicated to Rps2.

scholarly journals Tsr4 is a cytoplasmic chaperone for the ribosomal protein Rps2 in Saccharomyces cerevisiae

2019 ◽  
Author(s):  
Joshua J. Black ◽  
Sharmishtha Musalgaonkar ◽  
Arlen W. Johnson
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Ribosomal Protein ◽  
Unknown Function ◽  
Ribosomal Proteins ◽  
Ribosome Biogenesis ◽  
Eukaryotic Ribosome ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Nonspecific Interactions ◽  
Disordered Regions

AbstractEukaryotic ribosome biogenesis requires the action of approximately 200 trans-acting factors and the incorporation of 79 ribosomal proteins (RPs). The delivery of RPs to pre-ribosomes is a major challenge for the cell because RPs are often highly basic and contain intrinsically disordered regions prone to nonspecific interactions and aggregation. To counteract this, eukaryotes developed dedicated chaperones for certain RPs that promote their solubility and expression, often by binding eukaryotic-specific extensions of the RPs. Rps2 (uS5) is a universally conserved RP that assembles into nuclear pre-40S subunits. However, a chaperone for Rps2 had not been identified. Our lab previously characterized Tsr4 as a 40S biogenesis factor of unknown function. Here, we report that Tsr4 co-translationally associates with Rps2. Rps2 harbors a eukaryotic-specific N-terminal extension that was critical for its interaction with Tsr4. Moreover, Tsr4 perturbation resulted in decreased Rps2 levels and phenocopied Rps2 depletion. Despite Rps2 joining nuclear pre-40S particles, Tsr4 appeared to be restricted to the cytoplasmic. Thus, we conclude that Tsr4 is a cytoplasmic chaperone dedicated to Rps2.

scholarly journals Cavin1 intrinsically disordered domains are essential for fuzzy electrostatic interactions and caveola formation

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Vikas A. Tillu ◽  
James Rae ◽  
Ya Gao ◽  
Nicholas Ariotti ◽  
Matthias Floetenmeyer ◽  
...  
Keyword(s):  
Electrostatic Interactions ◽  
Membrane Lipid ◽  
Membrane Curvature ◽  
Caveolin 1 ◽  
Intrinsically Disordered ◽  
Intrinsically Disordered Regions ◽  
Solution Generation ◽  
Endosomal System ◽  
Disordered Regions

AbstractCaveolae are spherically shaped nanodomains of the plasma membrane, generated by cooperative assembly of caveolin and cavin proteins. Cavins are cytosolic peripheral membrane proteins with negatively charged intrinsically disordered regions that flank positively charged α-helical regions. Here, we show that the three disordered domains of Cavin1 are essential for caveola formation and dynamic trafficking of caveolae. Electrostatic interactions between disordered regions and α-helical regions promote liquid-liquid phase separation behaviour of Cavin1 in vitro, assembly of Cavin1 oligomers in solution, generation of membrane curvature, association with caveolin-1, and Cavin1 recruitment to caveolae in cells. Removal of the first disordered region causes irreversible gel formation in vitro and results in aberrant caveola trafficking through the endosomal system. We propose a model for caveola assembly whereby fuzzy electrostatic interactions between Cavin1 and caveolin-1 proteins, combined with membrane lipid interactions, are required to generate membrane curvature and a metastable caveola coat.

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