Hydrophilic Shell Matrix Proteins ofNautilus pompiliusand The Identification of a Core Set of Conchiferan Domains

Author:

Setiamarga Davin H. E.,Hirota Kazuki,Yoshida Masa-aki,Takeda Yusuke,Kito Keiji,Shimizu Keisuke,Isowa Yukinobu,Ikeo Kazuho,Sasaki Takenori,Endo Kazuyoshi

Abstract

AbstractDespite being a member of the shelled mollusks (Conchiferans), most members of extant cephalopods have lost their external biomineralized shells, except for the Nautiloids. Here, we report the result of our study to identify major Shell Matrix Proteins and their domains in the NautiloidNautilus pompilius, in order to gain a general insight into the evolution of Conchiferan Shell Matrix Proteins. In order to do so, we conducted transcriptomics of the mantle, and proteomics of the shell ofN. pompiliussimultaneously. Analyses of obtained data identified 61 distinct shell-specific sequences. Of the successfully annotated 27 sequences, protein domains were predicted in 19. Comparative analysis ofNautilussequences with four Conchiferans for which Shell Matrix Protein data were available (the pacific oyster, the pearl oyster, the limpet, and theEuhadrasnail) revealed that three proteins and six domains of the shell proteins are conserved in all Conchiferans. Interestingly, when the terrestrialEuhadrasnail was excluded, another five proteins and six domains were found to be shared among the four marine Conchiferans. Phylogenetic analyses indicated that most of these proteins and domains were present in the ancestral Conchiferan, but employed in shell formation later and independently in most clades. Although further studies utilizing deeper sequencing techniques to obtain genome and full-length sequences, and functional analyses, must be done in the future, our results here provide important pieces of information for the elucidation of the evolution of Conchiferan shells at the molecular level.

Publisher

Cold Spring Harbor Laboratory

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