Expression of foreign type I ribulose-1,5-bisphosphate carboxylase/ oxygenase (EC 4.1.1.39) stimulates photosynthesis in cyanobacterium Synechococcus PCC7942 cells

被引:0
作者
T. Iwaki
K. Haranoh
N. Inoue
K. Kojima
R. Satoh
T. Nishino
S. Wada
H. Ihara
S. Tsuyama
H. Kobayashi
A. Wadano
机构
[1] Osaka Prefecture University,Graduate Scholl of Life and Environmental Sciences
[2] Osaka Prefecture University,Graduate Scholl of Sciences
[3] University of Shizuoka,School of Food and Nutritional Sciences
来源
Photosynthesis Research | 2006年 / 88卷
关键词
overexpression; O; evolution; photosynthesis; RuBisCO;
D O I
暂无
中图分类号
学科分类号
摘要
A reporter gene assay revealed that promoters derived from Synechococcus PCC7942 (S.7942) psbAI and Synechocystis PCC6803 (S.6803) psbAII were suitable for the expression of foreign ribulose-bisphosphate carboxylase (RuBisCO; EC 4.1.1.39) in S.7942 cells. Transformational vectors with a promoter and a foreign RuBisCO gene, cvrbc originated from Allochromatium vinosum, were constructed on a binary vector, pUC303, and introduced to S.7942 cells. When the cvrbc was expressed with the S.7942 psbAI promoter, the total RuBisCO activity increased 2.5- to 4-fold than that of the wild type cell. The S.6803 psbAII promoter increased the activity of the transformant 1.5–2 times of that of wild type cell. There was a significant increase in the rate of photosynthesis depending on the increase of RuBisCO activity. The maximum rate of photosynthesis of the transformant cell was 1.63 times higher than that of the wild type under the illumination of 400 μmol m−2 s−1, at 20 mM bicarbonate and at 30 °C. Although the photosynthesis of the higher plant is limited by the ability of photosystems under high irradiance and the high CO2 concentration, that of the S.7942 cell is limited by the RuBisCO activity, even at high CO2 concentrations and under high irradiance.
引用
收藏
相关论文
共 86 条
  • [1] Alam J(1974)An improved spectrophotometric␣assay for ribulosebisphosphate carboxylase Biochim Biophys Acta 358 226-229
  • [2] Cook JL(1981)Kinetics and subunit interactions of ribulose bisphosphate carboxylase-oxygenase from the cyanobacterium, J Biol Chem 256 8445-8451
  • [3] Andrews TJ(1980) sp Arch Biochem Biophys 201 247-254
  • [4] Abel KM(1998)Kinetic properties of ribulose 1,5-bisphosphate carboxylase/oxygenase from Can J Bot 76 1052-1071
  • [5] Badger MR(2003)The diversity and coevolution of RuBisCO, plastids, pyrenoids, and chloroplast-based CO J Exp Bot 54 609-622
  • [6] Badger MR(1984)-concentrating mechanism in algae Planta 160 305-313
  • [7] Andrews TJ(1989)CO Arch Microbiol 151 59-64
  • [8] Whitney SM(1966)concentrating mechanisms in cyanobacteria: molecular components, their diversity and evolution Plant Physiol 111 725-734
  • [9] Ludwig M(1992)The relationship between steady-state gas exchange of bean leaves and the levels of carbon-reduction-cycle intermediates Plant Physiol 98 294-302
  • [10] Yellowlees DC(1970)Amplified expression of ribulose bisphosphate carboxylase/oxygenase in pBR 322-transformants of Nature 227 680-685