Whitney S M, Shaw D C, Yellowlees D
Department of Molecular Science, James Cook University, Queensland, Australia.
Proc Biol Sci. 1995 Mar 22;259(1356):271-5. doi: 10.1098/rspb.1995.0040.
The ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) large subunit from several dinoflagellates has a structure similar to that of the Form II enzyme from Rhodospirillum and Rhodobacter species rather than the Form I Rubisco of eukaryotic algae and higher plants. The dinoflagellate Rubisco was identified on native polyacrylamide gels by autoradiographic detection of the stable Rubisco-[2'-14C]-2-carboxy-D-arabinitol 1,5-bisphosphate complex. The antibody to the Symbiodinium sp. large subunit cross reacts with both the Rhodospirillum rubrum and Rhodobacter sphaeroides Form II enzyme whereas antibodies to the R. rubrum Rubisco cross react with a range of dinoflagellate Rubisco large subunits. The N-terminal amino acid sequence of the large subunit from both Symbiodinium sp. and Amphidinium carterae confirmed this relation. The lack of inhibition of the dinoflagellate Rubisco by 6-phosphogluconate is consistent with this structure.
几种甲藻的核酮糖-1,5-二磷酸羧化酶/加氧酶(Rubisco)大亚基,其结构与红螺菌属和红杆菌属物种的Ⅱ型酶相似,而非真核藻类和高等植物的Ⅰ型Rubisco。通过放射自显影检测稳定的Rubisco-[2'-14C]-2-羧基-D-阿拉伯糖醇1,5-二磷酸复合物,在天然聚丙烯酰胺凝胶上鉴定了甲藻的Rubisco。针对共生甲藻大亚基的抗体与深红红螺菌和球形红杆菌的Ⅱ型酶都有交叉反应,而针对深红红螺菌Rubisco的抗体与一系列甲藻Rubisco大亚基有交叉反应。共生甲藻和卡特亚得藻大亚基的N端氨基酸序列证实了这种关系。6-磷酸葡萄糖酸对甲藻Rubisco缺乏抑制作用与这种结构一致。