Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene
Maximum activity of recombinant ribulose 1,5-bisphosphate carboxylase/oxygenase of Anabaena sp. strain CA requires the product of the rbcX gene
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DOI：
10.1128/jb.179.11.3793-3796.1997
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发表时间：
1997-06-01
影响因子：
3.2
通讯作者：
Tabita, FR
中科院分区：
文献类型：
--
作者：
Li, LA;Tabita, FR
鱼腥藻属的丝状蓝藻含有一个独特的开放阅读框架rbcX，它是并列和共转录的，编码I核酮糖1，5-二磷酸羧基/加氧酶(Rubisco)的基因(rbcL和rbcs)。含鱼腥藻基因的质粒构建。在大肠杆菌中的表达研究表明，rbcX基因的产物模仿了伴侣蛋白促进重组Rubisco蛋白正确折叠的能力。纯化的重组鱼腥藻。菌株CA Rubisco，与其他蓝藻的Rubisco酶非常相似，在时间过程实验中被证明没有受到活性抑制，这种伴随的重组蛋白的性质似乎与从天然生物中分离的酶的性质一致。
Filamentous cyanobacteria of the genus Anabaena contain a unique open reading frame, rbcX, which is juxtaposed and cotranscribed,vith the genes (rbcL and rbcS) encoding form I ribulose 1,5-bisphosphate carboxylase/oxygenase (RubisCO). Plasmid constructions containing the genes from Anabaena sp. strain CA were prepared, and expression studies in Escherichia coli indicated that the product of the rbcX gene mimicked the ability of chaperonin proteins to facilitate the proper folding of recombinant RubisCO proteins. The purified recombinant Anabaena sp. strain CA RubisCO, much like the RubisCO enzymes from other cyanobacteria, was shown not to undergo inhibition of activity during a time course experiment, and the properties of this chaperoned recombinant protein appear to be consistent with those of the enzyme isolated from the native organism.