Proteome analysis of shell matrix proteins in the brachiopod Laqueus rubellus.

ABSTRACT:

Background

The calcitic brachipod shells contain proteins that play pivotal roles in shell formation and are important in understanding the evolution of biomineralization. Here, we performed a large-scale exploration of shell matrix proteins in the brachiopod Laqueus rubellus.

Results

A total of 40 proteins from the shell were identified. Apart from five proteins, i.e., ICP-1, MSP130, a cysteine protease, a superoxide dismutase, and actin, all other proteins identified had no homologues in public databases. Among these unknown proteins, one shell matrix protein was identified with a domain architecture that includes a NAD(P) binding domain, an ABC-type transport system, a transmembrane region, and an aspartic acid rich region, which has not been detected in other biominerals

SUBMITTER: Isowa Y 

PROVIDER: S-EPMC4536745 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature