title: cfMSP-1, an extremely acidic matrix protein involved in shell formation of the scallop Chlamys farreri.
abstract: Matrix proteins play an important role in biomineralization by mollusks. In this study, we cloned and characterized an acidic protein (pI=3.36) homolog of cfMSP-1 that is highly expressed in the mantle transcriptome of the scallop Chlamys farreri. RT-PCR and in situ hybridization showed that cfMSP-1 is specifically expressed in the outer fold of the mantle edge and pallial part. The expression level of cfMSP-1 remarkably increased and then reduced gradually to a value that is ~2-fold higher than basal levels after shell notching. Knock-down expression of cfMSP-1 in adults via dsRNA injection gave a disordered folia surface. Both shell notching and RNAi experiments indicated that cfMSP-1 plays an essential role in the formation of the folia of C. farreri.
authors.affiliation: Institute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Ganchu
authors.initials: G
authors.lastname: Jia
authors.affiliation: Institute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Jian
authors.initials: J
authors.lastname: Liang
authors.affiliation: Institute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Jun
authors.initials: J
authors.lastname: Xie
authors.affiliation: Institute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
authors.forename: Jun
authors.initials: J
authors.lastname: Wang
authors.affiliation: Key Laboratory of Marine Genetics and Breeding (MGB), Ministry of Education, College of Marine Life Sciences, Ocean University of China, Qingdao, China.
authors.forename: Zhenmin
authors.initials: Z
authors.lastname: Bao
authors.affiliation: Institute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China; Protein Science Laboratory of the Ministry of Education, Tsinghua University, Beijing 100084, China. Electronic address: lpxie@tsinghua.edu.cn.
authors.forename: Liping
authors.initials: L
authors.lastname: Xie
authors.affiliation: Institute of Marine Biotechnology, School of Life Sciences, Tsinghua University, Beijing 100084, China; Protein Science Laboratory of the Ministry of Education, Tsinghua University, Beijing 100084, China. Electronic address: rqzhang@mail.tsinghua.edu.cn.
authors.forename: Rongqing
authors.initials: R
authors.lastname: Zhang
mesh_terms: D000595:Amino Acid Sequence; D060105:Animal Shells / Q000378:metabolism*; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D005786:Gene Expression Regulation; D020868:Gene Silencing; D006023:Glycoproteins / Q000737:chemistry / Q000172:deficiency / Q000235:genetics / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008903:Minerals / Q000378:metabolism; D008969:Molecular Sequence Data; D049897:Pectinidae / Q000235:genetics / Q000378:metabolism*; D017421:Sequence Analysis
chemical_list: D018076:DNA, Complementary; D006023:Glycoproteins; D008903:Minerals
keywords: Biomineralization; Chlamys farreri; Shell; cfMSP-1