Boland M P, Taylor M F, Holmes C F
Department of Biochemistry, University of Alberta, Edmonton, Canada.
FEBS Lett. 1993 Nov 8;334(1):13-7. doi: 10.1016/0014-5793(93)81670-u.
The unicellular marine dinoflagellate, Prorocentrum lima, an established producer of okadaic acid (OA), was shown to contain a type-1 protein phosphatase (PP-1) the biochemical profile of which on Mono-Q and Superdex-75 fast protein liquid chromatography was identical to the catalytic subunit of PP-1 from rabbit skeletal muscle. Purified P. lima PP-1 (apparent molecular mass 37.5 kDa) was highly sensitive to inhibition by mammalian protein phosphatase inhibitor-1 and inhibitor-2, and to OA itself. A 6-7-fold increase in OA production by P. lima, when grown under controlled conditions, correlated with an up to 300-fold increase in P. lima PP-1 activity. Furthermore, P. lima did not contain any detectable type-2A protein phosphatase activity. This study represents the first identification of a serine/threonine protein phosphatase in a dinoflagellate.
单细胞海洋双鞭毛藻利马原甲藻（Prorocentrum lima）是一种已确定的冈田酸（OA）生产者，研究表明它含有一种1型蛋白磷酸酶（PP-1），该酶在Mono-Q和Superdex-75快速蛋白质液相色谱上的生化图谱与兔骨骼肌PP-1的催化亚基相同。纯化的利马原甲藻PP-1（表观分子量37.5 kDa）对哺乳动物蛋白磷酸酶抑制剂-1和抑制剂-2以及OA本身的抑制作用高度敏感。在受控条件下生长时，利马原甲藻产生的OA增加6-7倍，这与利马原甲藻PP-1活性高达300倍的增加相关。此外，利马原甲藻未检测到任何2A型蛋白磷酸酶活性。这项研究首次在双鞭毛藻中鉴定出丝氨酸/苏氨酸蛋白磷酸酶。
