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© Sandrine Etienne-Manneville
Photo prise à l'avant (dans la protrusion) d'astrocytes primaires de rat en migration. Marquage par immunofluorescence montrant en rouge, p150 Glued, une protéine associée aux extrémités 'plus' des microtubules et en vert la tubuline des microtubules. La photographie montre l'accumulation de p150 Glued à l'avant des cellules en migration, où la protéine pourrait participer à l'ancrage des microtubules à la membrane plasmique. Pour essayer de corriger, les dérèglements observés lors de la migration des cellules d'astrocytes tumuraux ou gliomes on cherche à connaitre les mécanismes moléculaires fondamentaux qui controlent la polarisation et la migration cellulaires.
Publication : Protein engineering

Does fusion of domains from unrelated proteins affect their folding pathways and the structural changes involved in their function? A case study with the diphtheria toxin T domain

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Protein engineering - 01 May 2002

Chenal A, Nizard P, Forge V, Pugnière M, Roy MO, Mani JC, Guillain F, Gillet D

Link to Pubmed [PMID] – 12034858

Protein Eng. 2002 May;15(5):383-91

We investigated whether the structural and functional behaviors of two unrelated protein domains were modified when fused. The IgG-binding protein ZZ derived from staphylococcal protein A was fused to the N- and/or C-terminus of the diphtheria toxin transmembrane domain (T). T undergoes a conformational change from a soluble native state at neutral pH to a molten globule-like state at acidic pH, leading to its interaction with membranes. We found that this molten globule state was not connected to the GdnHCl-induced unfolding pathway of T. The pH-induced transition of T, and also the unfolding of T and ZZ at neutral and acidic pH, were unchanged whether the domains were isolated or fused. The position of ZZ, however, influenced the solubility of T near its pK(i). SPR measurements revealed that T has a high affinity for membranes, isolated or within the fusion proteins (K(D)< 10(-11) M). This work shows that in the case of T and ZZ, the fusion of protein domains with different stabilities does not alter the structural changes involved in folding and function. This supports the use of T as a soluble membrane anchor.

https://www.ncbi.nlm.nih.gov/pubmed/12034858