Molecular cloning, expression and functional analysis of three subunits of protein phosphatase 2A (PP2A) from black tiger shrimps (Penaeus monodon)

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• 作者：Chao Zhao^a ; ^c ; ¹ ; Yan Wang^a ; ^b ; ¹ ; Mingjun Fu^a ; ^c ; Keng Yang^a ; Lihua Qiu^a ; ^d ; ^{qiugroup_bio@outlook.com}
• 关键词：Penaeus monodon ; Protein phosphatase 2A ; mRNA expression ; 5-Hydroxytryptamine and dopamine ; Phosphatase activity
• 刊名：Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：204
• 期：Complete
• 页码：77-89
• 全文大小：5522 K
• 卷排序：204

文摘

Protein phosphatase 2A (PP2A) is a cellular serine-threonine (Ser/Thr) phosphatase that plays a crucial role in regulating most cellular functions. In the present study, the full-length cDNAs of three subunits of PmPP2A (PmPP2A-A, PP2A-B and PP2A-C) were cloned from Penaeus monodon, which are the first available for shrimps. Sequence analysis showed that PmPP2A-A, PmPP2A-B and PmPP2A-C encoded polypeptides of 591, 443, and 324 amino acids, respectively. The mRNAs of three subunits of PmPP2A were expressed constitutively in all tissues examined, and predominantly in the ovaries. In ovarian maturation stages, the three subunits of PmPP2A were continuously but differentially expressed. Dopamine and 5-hydroxytryptamine injection experiments were conducted to study the expression profile of three subunits of PmPP2A, and the results indicated that PmPP2A played a negative regulatory role in the process of ovarian maturation. In addition, the recombinant proteins of three subunits of PmPP2A were successfully obtained, and the phosphatase activity of PmPP2A was tested in vitro. The results of this study will advance our understanding about the molecular mechanisms of PmPP2A in Penaeus monodon.