Salt Dependence Conformational Stability of the Dimeric
SAM Domain of MAPKKK Ste11 from Budding Yeast: A Native-State H/D
Exchange NMR Study
Posted on 2020-07-27 - 15:07
The
sterile α motif, also called the SAM domain, is known
to form homo or heterocomplexes that modulate diverse biological functions
through the regulation of specific protein–protein interactions.
The MAPK pathway of budding yeast Saccharomyces cerevisiae is comprised of a three-tier kinase system akin to mammals. The
MAPKKK Ste11 protein of yeast contains a homodimer SAM domain, which
is critical for transmitting cues to the downstream kinases. The structural
stability of the dimeric Ste11 SAM is maintained by hydrophobic and
ionic interactions at the interfacial amino acids. The urea-induced
equilibrium-unfolding process of the Ste11 SAM domain is cooperative
without evidence of any intermediate states. The native-state H/D
exchange under subdenaturing conditions is a useful method for the
detection of intermediate states of proteins. In the present study,
we investigated the effect of ionic strength on the conformational
stability of the dimer using the H/D exchange experiments. The hydrogen
exchange behavior of the Ste11 dimer under physiological salt concentrations
reveals two partially unfolded metastable intermediate states, which
may be generated by a sequential and cooperative unfolding of the
five helices present in the domain. These intermediates appear to
be significant for the reversible unfolding kinetics via hydrophobic
collapse. In contrast, higher ionic concentrations eliminate this
cooperative interactions that stabilize the pairs of helices.
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Bhunia, Anirban; Ilyas, Humaira; Bhattacharjya, Surajit (2020). Salt Dependence Conformational Stability of the Dimeric
SAM Domain of MAPKKK Ste11 from Budding Yeast: A Native-State H/D
Exchange NMR Study. ACS Publications. Collection. https://doi.org/10.1021/acs.biochem.0c00522