N′-terminal- and Ca2+-induced stabilization of high-order oligomers of full-length Danio rerio and Homo sapiens otolin-1

The Role of Intrinsically Disordered Proteins in Liquid–Liquid Phase Separation during Calcium Carbonate Biomineralization

“…Otolin-1 is composed of four domains: a 23-amino acid signal peptide, a non-collagenous N-terminal domain, a central collagen-like domain, and a globular C-terminal C1q domain liable for protein molecule trimerization [ 89 ]. The presence of calcium ions influences the secondary and tertiary structure of recombinant otolin-1, especially the thermal stability [ 90 ]. Recombinant human and zebrafish otolin-1 forms high-order oligomers [ 90 ].…”

“…The presence of calcium ions influences the secondary and tertiary structure of recombinant otolin-1, especially the thermal stability [ 90 ]. Recombinant human and zebrafish otolin-1 forms high-order oligomers [ 90 ]. The oligomerization of zebrafish protein is dependent on its concentration and the presence of calcium ions, whereas human protein exhibits the same oligomeric stage regardless of these factors.…”

“…The oligomerization of zebrafish protein is dependent on its concentration and the presence of calcium ions, whereas human protein exhibits the same oligomeric stage regardless of these factors. Despite the high sequence similarity (45.51% identity and 56.58% similarity), these two homologues show differences that may be reflected in the nature of otoliths and otoconia [ 90 ]. Otolin-1 could be the crucial element of the organic matrix of otoconia and otoliths, serving as a high-order oligomeric scaffolding protein stabilized by calcium ions [ 90 ].…”

“…Despite the high sequence similarity (45.51% identity and 56.58% similarity), these two homologues show differences that may be reflected in the nature of otoliths and otoconia [ 90 ]. Otolin-1 could be the crucial element of the organic matrix of otoconia and otoliths, serving as a high-order oligomeric scaffolding protein stabilized by calcium ions [ 90 ].…”