RuBisCO-like proteins as the enolase enzyme in the methionine salvage pathway: functional and evolutionary relationships between RuBisCO-like proteins and photosynthetic RuBisCO

被引:41
作者
Ashida, Hiroki [1 ]
Saito, Yohtaro [1 ]
Nakano, Toshihiro [1 ]
de Marsac, Nicole Tandeau [2 ]
Sekowska, Agnieszka [3 ]
Danchin, Antoine [4 ]
Yokota, Akiho [1 ]
机构
[1] Nara Inst Sci & Technol, Grad Sch Biol Sci, Nara 6300101, Japan
[2] Inst Pasteur, CNRS, URA 2172, Unite Cyanobacteries, F-75724 Paris 15, France
[3] Inst Pasteur, Unite Genet Silico, F-75724 Paris 15, France
[4] Inst Pasteur, CNRS, URA 2171, F-75724 Paris 15, France
关键词
Bacillus subtilis; CO2; fixation; 2,3-diketo-5-methylthiopentyl-1-phosphate enolase; methionine salvage pathway; molecular evolution; photosynthesis; RuBisCO; RuBisCO-like protein;
D O I
10.1093/jxb/ern104
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) is the key enzyme in the fixation of CO2 in the Calvin cycle of plants. Many genome projects have revealed that bacteria, including Bacillus subtilis, possess genes for proteins that are similar to the large subunit of RuBisCO. These RuBisCO homologues are called RuBisCO-like proteins (RLPs) because they are not able to catalyse the carboxylase or the oxygenase reactions that are catalysed by photosynthetic RuBisCO. It has been demonstrated that B. subtilis RLP catalyses the 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) enolase reaction in the methionine salvage pathway. The structure of DK-MTP-1-P is very similar to that of ribulose-1,5-bisphosphate (RuBP) and the enolase reaction is a part of the reaction catalysed by photosynthetic RuBisCO. In this review, functional and evolutionary relationships between B. subtilis RLP of the methionine salvage pathway, other RLPs, and photosynthetic RuBisCO are discussed. In addition, the fundamental question, 'How has RuBisCO evolved?' is also considered, and evidence is presented that RuBisCOs evolved from RLPs.
引用
收藏
页码:1543 / 1554
页数:12
相关论文
共 43 条
[1]  
Andrews T.J., 1987, BIOCH PLANTS, P131, DOI 10.1016/B978-0-12-675410-0.50009-9
[2]   Manipulating ribulose bisphosphate carboxylase/oxygenase in the chloroplasts of higher plants [J].
Andrews, TJ ;
Whitney, SM .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2003, 414 (02) :159-169
[3]  
[Anonymous], 2002, Bacillus subtilis and its closest relatives
[4]   Was photosynthetic RuBisCO recruited by acquisitive evolution from RuBisCO-like proteins involved in sulfur metabolism? [J].
Ashida, H ;
Danchin, A ;
Yokota, A .
RESEARCH IN MICROBIOLOGY, 2005, 156 (5-6) :611-618
[5]   A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO [J].
Ashida, H ;
Saito, Y ;
Kojima, C ;
Kobayashi, K ;
Ogasawara, N ;
Yokota, A .
SCIENCE, 2003, 302 (5643) :286-290
[6]  
BALAKRISHNAN R, 1993, J BIOL CHEM, V268, P24792
[7]   Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis [J].
Berger, BJ ;
English, S ;
Chan, G ;
Knodel, MH .
JOURNAL OF BACTERIOLOGY, 2003, 185 (08) :2418-2431
[8]   The role of methionine recycling for ethylene synthesis in Arabidopsis [J].
Buerstenbinder, Katharina ;
Rzewuski, Guillaume ;
Wirtz, Markus ;
Hell, Ruediger ;
Sauter, Margret .
PLANT JOURNAL, 2007, 49 (02) :238-249
[9]   A new Rubisco-like protein coexists with a photosynthetic Rubisco in the planktonic cyanobacteria Microcystis [J].
Carre-Mlouka, Alyssa ;
Mejean, Annick ;
Quillardet, Philippe ;
Ashida, Hiroki ;
Saito, Yohtaro ;
Yokota, Akiho ;
Callebaut, Isabelle ;
Sekowska, Agnieszka ;
Dittmann, Elke ;
Bouchier, Christiane ;
de Marsac, Nicole Tandeau .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (34) :24462-24471
[10]   Mechanism of Rubisco: The carbamate as general base [J].
Cleland, WW ;
Andrews, TJ ;
Gutteridge, S ;
Hartman, FC ;
Lorimer, GH .
CHEMICAL REVIEWS, 1998, 98 (02) :549-561