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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. We also identified pectin lyase-like, trypsin inhibitor, and saposin B functional domains in the amino acid sequences of the shell matrix proteins. The repertoire of brachiopod shell matrix proteins also contains two basic amino acid-rich proteins and proteins that have a variety of repeat sequences. CONCLUSIONS:Our study suggests an independent origin and unique mechanisms for brachiopod shell formation.

SUBMITTER: Isowa Y 

PROVIDER: S-EPMC4536745 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature

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

Isowa Yukinobu Y   Sarashina Isao I   Oshima Kenshiro K   Kito Keiji K   Hattori Masahira M   Endo Kazuyoshi K  

Proteome science 20150815


<h4>Background</h4>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.<h4>Results</h4>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 homo  ...[more]

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