Recombinant transgelin-like protein 1 from Mytilus shell induces formation of CaCO₃ polymorphic crystals in vitro.

ABSTRACT: Transgelin is an actin cross-linking/gelling protein of the calponin family, which is associated with actin stress fibres, cell motility, adhesion and the maintenance of cell morphology. Transgelin-like proteins (TLPs) have also been identified as shell matrix proteins (SMPs) in several mollusc species; however, the functions of TLPs in biomineralization remain unknown. Transgelin-like protein 1 (TLP-1) was previously identified from the shell of Mytilus coruscus as a novel 19 kDa SMP with a calponin homology (CH) domain. To understand the role of TLP-1 in shell formation, the expression level and localization of the TLP-1 gene in biomineralization-related tissues were determined in this study. Furthermore, recombinant TLP-1 was expressed in a prokaryotic expression system with codon optim

SUBMITTER: Jiang Y 

PROVIDER: S-EPMC7530383 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature