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Distinct form I, II, III, and IV Rubisco proteins from the three kingdoms of life provide clues about Rubisco evolution and structure/function relationships

机译:来自三个生命王国的不同形式I,II,III和IV Rubisco蛋白提供了关于Rubisco进化以及结构/功能关系的线索

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摘要

There are four forms of ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) found in nature. Forms I, II, and III catalyse the carboxylation and oxygenation of ribulose 1,5-bisphosphate, while form IV, also called the Rubisco-like protein (RLP), does not catalyse either of these reactions. There appear to be six different clades of RLP. Although related to bona fide Rubisco proteins at the primary sequence and tertiary structure levels, RLP from two of these clades is known to perform other functions in the cell. Forms I, II, and III Rubisco, along with form IV (RLP), are thought to have evolved from a primordial archaeal Rubisco. Structure/function studies with both archaeal form III (methanogen) and form I (cyanobacterial) Rubisco have identified residues that appear to be specifically involved with interactions with molecular oxygen. A specific region of all form I, II, and III Rubisco was identified as being important for these interactions.
机译:自然界中存在四种形式的核糖1,5-二磷酸羧化酶/加氧酶(Rubisco)。形式I,II和III催化核糖1,5-双磷酸的羧化和氧合,而形式IV(也称为Rubisco样蛋白(RLP))不催化这两个反应。 RLP似乎有六个不同的分支。尽管在一级序列和三级结构水平上与真正的Rubisco蛋白有关,但是已知其中两个进化枝的RLP在细胞中具有其他功能。形式I,II和III Rubisco与形式IV(RLP)一起被认为是从原始古细菌Rubisco演变而来的。对古细菌III型(甲烷)和I型(蓝细菌)Rubisco进行结构/功能研究,已鉴定出似乎与分子氧相互作用特别相关的残基。所有形式的I,II和III Rubisco的特定区域都被认为对这些相互作用很重要。

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    《Journal of Experimental Botany》 |2008年第7期|p.1515-1524|共10页
  • 作者单位

    1Department of Microbiology, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210–1292, USA 2The Plant Molecular Biology Biology/Biotechnology Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210–1292, USA 3The OSU Biochemistry Program, The Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210–1292, USA 4College of Marine and Earth Studies, Delaware Biotechnology Institute, University of Delaware, 127 DBI, 15 Innovation Way, Newark, DE 19711, USA;

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