The RING domain of the scaffold protein Ste5 adopts a molten globular character with high thermal and chemical stability.
Angew Chem Int Ed Engl
; 53(5): 1320-3, 2014 Jan 27.
Article
in En
| MEDLINE
| ID: mdl-24356903
ABSTRACT
Ste5 is a scaffold protein that controls the pheromone response of the MAP-kinase cascade in yeast cells. Upon pheromone stimulation, Ste5 (through its RING-H2 domain) interacts with the ß and γ subunits of an activated heterodimeric Gâ
protein and promotes activation of the MAP-kinase cascade. With structural and biophysical studies, we show that the Ste5 RING-H2 domain exists as a molten globule under native buffer conditions, in yeast extracts, and even in denaturing conditions containing urea (7 M). Furthermore, it exhibits high thermal stability in native conditions. Binding of the Ste5 RING-H2 domain to the physiological Gß/γ (Ste4/Ste18) ligand is accompanied by a conformational transition into a better folded, more globular structure. This study reveals novel insights into the folding mechanism and recruitment of binding partners by the Ste5 RING-H2 domain. We speculate that many RING domains may share a similar mechanism of substrate recognition and molten-globule-like character.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Saccharomyces cerevisiae Proteins
/
Adaptor Proteins, Signal Transducing
Language:
En
Journal:
Angew Chem Int Ed Engl
Year:
2014
Type:
Article