Marc Quinternet (UMS IBSLor) and several members of IMoPA team 1 (S. Dermouche, M-E. Chagot and X. Manival) demonstrated that clever amino acid substitutions in the TPR1 domain of the SPAG1 protein, involved in the mechanisms of ciliogenesis in human, could drastically increase its solubility and stability.

This allowed the structural study on the B2S Core Facility (DLS, ITC and NMR) of this domain with the molecular chaperones HSP70 and HSP90, both required for the correct assembly of the dynein arms. It deciphers, at the atomic scale, the recognition modes between these protein partners.

This work, published in the journal Biochemistry, demonstrates the efficiency of protein sequence optimization for structural studies.

Publication: Dermouche S, Chagot ME, Manival X, Quinternet M. Optimizing the First TPR Domain of the Human SPAG1 Protein Provides Insight into the HSP70 and HSP90 Binding Properties. Biochemistry. 2021 Mar 19.

• DOI: 10.1021/acs.biochem.1c00052
• PUBMED: 33739091
• HAL: HAL-03175986