Poly(Adp-Ribose) Drives Condensation of Fus Via a Transient Interaction

2021 ◽  
Author(s):  
Kevin Rhine ◽  
Morgan Dasovich ◽  
Joseph Yoniles ◽  
Mohsen Badiee ◽  
Sophie Skanchy ◽  
...  
FEBS Letters ◽  
2018 ◽  
Vol 592 (9) ◽  
pp. 1464-1472 ◽  
Author(s):  
Matteo Rovere ◽  
John B. Sanderson ◽  
Luis Fonseca‐Ornelas ◽  
Dushyant S. Patel ◽  
Tim Bartels

2018 ◽  
Vol 30 (4) ◽  
pp. 046102 ◽  
Author(s):  
Warrick A. Miller ◽  
Paul R. Medwell ◽  
Con J. Doolan ◽  
Minkwan Kim

1992 ◽  
Vol 12 (11) ◽  
pp. 5059-5068 ◽  
Author(s):  
R Shaknovich ◽  
G Shue ◽  
D S Kohtz

A murine cardiac lambda gt11 expression library was screened with an amphipathic helix antibody, and a recombinant representing the C-terminal 194 residues of murine HSP90 (HSP84) was cloned. Both recombinant and native HSP90s were then found to rapidly convert a basic helix-loop-helix protein (MyoD1) from an inactive to an active conformation, as assayed by sequence-specific DNA binding. The conversion process involves a transient interaction between HSP90 and MyoD1 and does not result in the formation of a stable tertiary complex. Conversion does not require ATP and occurs stoichiometrically in a dose-dependent fashion. HSP90 is an abundant, ubiquitous, and highly conserved protein present in most eukaryotic cells. These results provide direct evidence that HSP90 can affect the conformational structure of a DNA-binding protein.


2008 ◽  
Vol 75 (3) ◽  
pp. 275-290 ◽  
Author(s):  
David J. Chappell ◽  
Paul J. Harris ◽  
David Henwood ◽  
Roma Chakrabarti

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