ASSEMBLY IN ESCHERICHIA-COLI OF A FUNCTIONAL MULTI-SUBUNIT RIBULOSE BISPHOSPHATE CARBOXYLASE FROM A BLUE-GREEN-ALGA
ASSEMBLY IN ESCHERICHIA-COLI OF A FUNCTIONAL MULTI-SUBUNIT RIBULOSE BISPHOSPHATE CARBOXYLASE FROM A BLUE-GREEN-ALGA
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DOI：
10.1038/314617a0
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发表时间：
1985-01-01
期刊：
影响因子：
64.8
通讯作者：
BRADLEY, D
中科院分区：
文献类型：
--
作者：
GATENBY, AA;VANDERVIES, SM;BRADLEY, D
酶核酮糖1，5-二磷酸羧化酶-加氧酶（RuBPCase）在光合生物中具有关键作用，催化光合作用和光呼吸互锁但相反的途径的第一反应1，2。农业上对RuBPCase的兴趣集中在改变酶结构以提高净光合产量的可能性上，但这种研究受到植物中十六聚体全酶结构复杂性的阻碍，这显然是由于大亚基的性质3，4。我们选择在大肠杆菌中表达蓝细菌SynechococcusPCC 6301的大小亚基基因，开发了一个实验系统，在该系统中，可以评估亚基组装后引入RuBPC酶多肽的结构变化。蓝细菌（蓝绿藻）是一种具有植物样光合机制和RuBPCase结构的自养原核生物5，6。我们在这里报告的活性RuBPCase inE的合成。大肠杆菌中含有大小亚基多肽。
The enzyme ribulose 1,5-bisphosphate carboxylase-oxygenase (RuBPCase) has a pivotal role in photosynthetic organisms, catalysing the first reactions of the interlocked but opposing pathways of photosynthesis and photorespiration1,2. The agricultural interest in RuBPCase centres on the possibility of altering the structure of the enzyme to improve net photosynthetic yield, but such studies are hampered by the structural complexity of the hexadecameric holoenzyme in plants which preventsin vitrodissociation and reconstitution, apparently due to the properties of the large subunits3,4. We have chosen to express the large and small subunit genes of the cyanobacteriumSynechococcusPCC6301 inEscherichia colito develop an experimental system in which structural changes introduced into RuBPCase polypeptides could be assessed following subunit assembly. The cyanobacteria (blue-green algae) are autotrophic prokaryotes which have a plant-like photosynthetic mechanism and RuBPCase structure5,6. We report here the synthesis of an active RuBPCase inE. coliwhich contains both large and small subunit polypeptides.