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Molecular Cloning of Calmodulin-like Protein Gene CaLP and Comparison with Expression Profiles of CaM Gene in Scallop Chlamys f arreri |
LIN Ya,LI Shi-guo,XIE Li-ping,ZHANG Rong-qing |
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Abstract T he formation of mollusk shells as products of calcium metabolism is a very complicated process highly controlled by many physiological and biochemical activities .However ,the regulation of calcium me‐tabolism in bivalves is poorly understood .In this study ,a calmodulin‐like protein CaLP was cloned from the mantle tissue of scallop Chlamys f arreri .The full‐length cDNA of CaLP was 863 bp ,including a 450‐bp open reading frame (ORF) ,encoding 149 aa with 17 .0 ku and pI of 4 .03 .CaLP was found to contain four putative EF‐hand domains ,with the ability of Ca2+‐binding ,and 66% identity with the C . f arreri CaM in the amino sequence .The scallop CaLP mRNA was expressed in all tissues tested ,with the maxi‐mal level in the mantle ,a key organ involved in calcium secretion and shell formation ,indicating that CaLP takes an important part in the calcium metabolic process of the scallop .Moreover ,the expression of CaLP gene in the mantle went up and came down along with the elevated Ca2+ concentration ,and then reached a climax with a moderate (30% ) increase in Ca2+ concentration ,indicating that the suitable Ca2+ concentra‐tion accelerated the high expression of CaLP gene ,otherwise ,it inhibited the expression of CaLP gene . The function of CaLP in biomineralization was investigated in a shell notching experiment .It was found that the expression of CaLP was greatly enhanced in the mantle tissue in the notched shells ,implying that CaLP was involved in the shell regeneration .The findings will provide useful information for further stud‐ies on function of CaLP gene as well as the biomineralization process in the scallop .
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Received: 25 November 2014
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