鲁比斯科
生物发生
光合作用
生物
蓝藻
细胞生物学
叶绿体
加氧酶
红色红螺菌
丙酮酸羧化酶
生物化学
核酮糖
伴随蛋白
酶
细菌
蛋白质折叠
遗传学
基因
作者
Thomas R. Hauser,Leonhard Popilka,F. Ulrich Hartl,Manajit Hayer‐Hartl
出处
期刊:Nature plants
[Nature Portfolio]
日期:2015-06-01
卷期号:1 (6): 15065-15065
被引量:194
标识
DOI:10.1038/nplants.2015.65
摘要
Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyses the conversion of atmospheric CO2 into organic compounds during photosynthesis. Despite its pivotal role in plant metabolism, Rubisco is an inefficient enzyme and has therefore been a key target in bioengineering efforts to improve crop yields. Much has been learnt about the complex cellular machinery involved in Rubisco assembly and metabolic repair over recent years. The simple form of Rubisco found in certain bacteria and dinoflagellates comprises two large subunits, and generally requires the chaperonin system for folding. However, the evolution of hexadecameric Rubisco, which comprises eight large and eight small subunits, from its dimeric precursor has rendered Rubisco in most plants, algae, cyanobacteria and proteobacteria dependent on an array of additional factors. These auxiliary factors include several chaperones for assembly as well as ATPases of the AAA+ family for functional maintenance. An integrated view of the pathways underlying Rubisco biogenesis and repair will pave the way for efforts to improve the enzyme with the goal of increasing crop yields.
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