Cloning and characterization of a novel G protein beta-subunit of pearl oyster (Pinctada fucata), and its interaction sites with calmodulin | |
Chen, L ; Xie, LP ; Xiong, XH ; Dai, YP ; Fan, WM ; Zhang, RQ | |
2010-05-11 ; 2010-05-11 ; OCT | |
关键词 | pinctada fucata G protein subunit gene calmodulin alkaline phosphatase ALKALINE-PHOSPHATASE ACTIVITY GTP-BINDING PROTEINS GAMMA-SUBUNITS PEPTIDE NACRE Biochemistry & Molecular Biology Zoology |
中文摘要 | A cDNA clone encoding a novel G protein beta subunit of beta(1) subclass, pfG beta(1) was isolated from the pearl oyster (Pinctada fucata). The deduced amino acid sequence of pfG beta(1) (341 amino acids) shares high homology to northern European squid (Loligo pealei) and great pond snail (Lymnaea stagnalis) G beta(1), while it has diverged from bovine (Bos taurus) and human. The well-conserved amino acid domains in G protein beta subunit, seven WD repeats, were founded in the deduced amino acid sequence. Alignment analysis showed that the beginning amino acid residues in variable fragment of the seventh WD motif are different from any other G beta. The prediction of 3D structure of pfG beta showed that pfG beta belongs to beta-propeller family proteins whose members contain 4-8 antiparallel p-sheets resembling the blades of a propeller. In situ hybridization and Northern blotting analysis revealed that the pfCi mRNA hybridization signals were widely expressed in various tissues except muscle, with abundantly in epithelia of gill, gonad and outer fold of mantle. We also investigated the interactions between G beta gamma and calmodulin (CaM), and specific amino acid residues that may be critical for the binding of G beta gamma to CaM were also identified. Furthermore, the functional studies of the interaction showed that the binding of CaM and G beta gamma increases the alkaline phosphatase (ALP) activity, an indicator for mineralization in MC3T3-E1 cells. The ALP activity of the mutants of pfG beta gamma that impaired the interactions of G beta gamma with CaM is higher than the Control group; however, it is lower than the WTC group. Together, these results suggest that the G beta gamma might interact with CaM and point to the important physiological function in modulating cellular functions. (c) 2005 Elsevier Inc. All rights reserved. |
语种 | 英语 ; 英语 |
出版者 | ELSEVIER SCIENCE INC ; NEW YORK ; 360 PARK AVE SOUTH, NEW YORK, NY 10010-1710 USA |
内容类型 | 期刊论文 |
源URL | [http://hdl.handle.net/123456789/26998] |
专题 | 清华大学 |
推荐引用方式 GB/T 7714 | Chen, L,Xie, LP,Xiong, XH,et al. Cloning and characterization of a novel G protein beta-subunit of pearl oyster (Pinctada fucata), and its interaction sites with calmodulin[J],2010, 2010, OCT. |
APA | Chen, L,Xie, LP,Xiong, XH,Dai, YP,Fan, WM,&Zhang, RQ.(2010).Cloning and characterization of a novel G protein beta-subunit of pearl oyster (Pinctada fucata), and its interaction sites with calmodulin.. |
MLA | Chen, L,et al."Cloning and characterization of a novel G protein beta-subunit of pearl oyster (Pinctada fucata), and its interaction sites with calmodulin".(2010). |
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