Characteristics of a Novel Tyrosinase Gene Involved in the Formation of Shell Color in Hard Clam Meretrix meretrix

Yao, Hanhan; Cui, Baoyue; Li, Xiaoying; Zhang, Lin; Dong, Yan

doi:10.1007/s11802-020-4202-1

Cited by 9 publications

(6 citation statements)

References 27 publications

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“…The VWA domain is known to function in protein-protein interaction, while Chitin-binding domain is known to interact with calcium ions in calcium carbonate [ 49 ]. Tyrosinase (both as a protein and a domain) is known to be involved in pigmentation [ 51 , 52 ], and found in all mollusks compared in this study. The protein was probably recruited to form the diverse coloration and color patterns of the shell.…”

Section: Discussionmentioning

confidence: 92%

Hydrophilic Shell Matrix Proteins of Nautilus pompilius and the Identification of a Core Set of Conchiferan Domains

Setiamarga

Hirota

Yoshida

et al. 2021

Genes

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Despite being a member of the shelled mollusks (Conchiferans), most members of extant cephalopods have lost their external biomineralized shells, except for the basally diverging Nautilids. Here, we report the result of our study to identify major Shell Matrix Proteins and their domains in the Nautilid Nautilus pompilius, in order to gain a general insight into the evolution of Conchiferan Shell Matrix Proteins. In order to do so, we performed a multiomics study on the shell of N. pompilius, by conducting transcriptomics of its mantle tissue and proteomics of its shell matrix. Analyses of obtained data identified 61 distinct shell-specific sequences. Of the successfully annotated 27 sequences, protein domains were predicted in 19. Comparative analysis of Nautilus sequences with four Conchiferans for which Shell Matrix Protein data were available (the pacific oyster, the pearl oyster, the limpet and the Euhadra snail) revealed that three proteins and six protein domains were conserved in all Conchiferans. Interestingly, when the terrestrial Euhadra snail was excluded, another five proteins and six protein domains were found to be shared among the four marine Conchiferans. Phylogenetic analyses indicated that most of these proteins and domains were probably present in the ancestral Conchiferan, but employed in shell formation later and independently in most clades. Even though further studies utilizing deeper sequencing techniques to obtain genome and full-length sequences, and functional analyses, must be carried out in the future, our results here provide important pieces of information for the elucidation of the evolution of Conchiferan shells at the molecular level.

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Section: Discussionmentioning

confidence: 92%

Hydrophilic Shell Matrix Proteins of Nautilus pompilius and the Identification of a Core Set of Conchiferan Domains

Setiamarga

Hirota

Yoshida

et al. 2021

Genes

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“…To date, studies of the involvement of TYR in shell color formation has also been widely reported, including studies in C. gigas [42,43], P. yessoensis [29], M. meretrix [44], P. fucata [45], and R. philippinarum [46]. In this study, qRT-PCR results showed that the mRNA of the TYR gene was widely expressed in all tissues of C. sinensis, with the highest and most signifcant expression in the outer mantle.…”

Section: Discussionmentioning

confidence: 54%

“…Te tyrosinase family has also been reported to be involved in melanin formation in Patinopecten yessoensis [29]. Tere were signifcant diferences in the expression level of TYR and the total melanin content at the edge of the mantle in M. meretrix with three diferent shell colors, indicating that TYR was involved in the formation of shell color [44]. Te TYR gene was shown to be involved in the wound healing process of P. fucata by specifc expression in mantle tissue, and this expression was speculated to be involved in the formation of the cuticle and prismatic layer of P. fucata [45].…”

Section: Discussionmentioning

confidence: 97%

“…[34][35][36][37], usually manifested as albinism [38] or abnormal visual function of the eyes [39][40][41]. In addition, studies of the TYR gene in bivalves has also been widely reported, including studies in C. gigas [42,43], P. yessoensis [29], Meretrix meretrix [44], Pinctada fucata [45], and Ruditapes philippinarum [46]. However, the TYR gene has not been reported in C. sinensis.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cloning, Characterization, and Expression Prolife Analysis of Tyrosinase Genes: Insights into Black Shell Formation in Cyclina sinensis

Sun¹,

Shan²,

Li³

et al. 2023

Aquaculture Research

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Shell colors that exhibit a positive relationship with excellent traits can be employed as marker colors for breeding new varieties of bivalves. The clam Cyclina sinensis is an economically important marine bivalve that has three main colors: black, white, and purple. In the present study, we cloned and analyzed the full-length cDNA of the tyrosinase gene (TYR), which is the key gene for melanin synthesis, to explore the formation mechanism of black shells. The full-length cDNA of TYR was cloned by RACE-PCR, and the results showed that the full-length cDNA of TYR was 2993 bp, including a 2262 bp open reading frame encoding 753 amino acids. The results of functional domain prediction showed that deduced TYR protein contains a typical functional domain of tyrosinase, the common central domain. Phylogenetic analysis was conducted using neighbor-joining and maximum likelihood methods, and the results indicated that the evolutionary positions of C. sinensis and Meretrix meretrix were closest. The qRT‒PCR results showed that TYR mRNA was highly expressed in the outer edge of the mantle, which suggested that TYR was involved in the synthesis of melanin in the mantle of C. sinensis and might play an important regulatory role in the formation of melanin in black clam shells.

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“…VWA domain has function of the protein-protein interaction, Chitin-binding domain has the interaction with calcium ions in calcium carbonate (Suzuki et al, 2011). Meanwhile, Tyrosinase (both as a protein and a domain) is known to be involved in pigmentation (Nagai et al, 2007; Yao et al, 2020), and found in all mollusks compared in this study. Tyrosinase involvement in pigmentation is not only in the shell, but the protein was probably recruited and included inside the shell matrices to form the diverse coloration and patterns of the shell.…”

Section: Discussionmentioning

confidence: 65%

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

Setiamarga

Hirota

Yoshida

et al. 2020

Preprint

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Despite 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 Nautiloid Nautilus 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 of N. pompilius simultaneously. Analyses of obtained data identified 61 distinct shell-specific sequences. Of the successfully annotated 27 sequences, protein domains were predicted in 19. Comparative analysis of Nautilus sequences with four Conchiferans for which Shell Matrix Protein data were available (the pacific oyster, the pearl oyster, the limpet, and the Euhadra snail) revealed that three proteins and six domains of the shell proteins are conserved in all Conchiferans. Interestingly, when the terrestrial Euhadra snail 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.

show abstract

Characteristics of a Novel Tyrosinase Gene Involved in the Formation of Shell Color in Hard Clam Meretrix meretrix

Cited by 9 publications

References 27 publications

Hydrophilic Shell Matrix Proteins of Nautilus pompilius and the Identification of a Core Set of Conchiferan Domains

Hydrophilic Shell Matrix Proteins of Nautilus pompilius and the Identification of a Core Set of Conchiferan Domains

Cloning, Characterization, and Expression Prolife Analysis of Tyrosinase Genes: Insights into Black Shell Formation in Cyclina sinensis

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

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