Volume 32 Issue 5
Sep.  2015
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WANG Chaoli, ZHANG Zhijun, QU Yaping, WANG Lei. Cloning, expression and purification of pyruvate, orthophosphate dikinase regulatory proteins from Phyllostachys edulis[J]. Journal of Zhejiang A&F University, 2015, 32(5): 749-755. doi: 10.11833/j.issn.2095-0756.2015.05.014
Citation: WANG Chaoli, ZHANG Zhijun, QU Yaping, WANG Lei. Cloning, expression and purification of pyruvate, orthophosphate dikinase regulatory proteins from Phyllostachys edulis[J]. Journal of Zhejiang A&F University, 2015, 32(5): 749-755. doi: 10.11833/j.issn.2095-0756.2015.05.014

Cloning, expression and purification of pyruvate, orthophosphate dikinase regulatory proteins from Phyllostachys edulis

doi: 10.11833/j.issn.2095-0756.2015.05.014
Funds:

国家自然科学基金资助项目(31270715);浙江省自然科学基金资助项目(LY14C160009)

  • Received Date: 2014-11-28
  • Rev Recd Date: 2015-01-09
  • Publish Date: 2015-10-20
通讯作者: 陈斌, bchen63@163.com
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    沈阳化工大学材料科学与工程学院 沈阳 110142

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Cloning, expression and purification of pyruvate, orthophosphate dikinase regulatory proteins from Phyllostachys edulis

doi: 10.11833/j.issn.2095-0756.2015.05.014
Funds:

国家自然科学基金资助项目(31270715);浙江省自然科学基金资助项目(LY14C160009)

Abstract: Pyruvate orthophosphate dikinase regulatory protein (PPDK-RP) is a key protein in C4 photosynthesis and can modified enzyme activity of PPDK. For Phyllostachys edulis, an important economic bamboo species, cloning PPDK-RP gene and studying its functions had vital theoretical value and application for bamboo photosynthesis research. Firstly PeRP1 was successfully cloned by reverse transcription polymerase chain reaction (RT-PCR), and afterward a multiple sequence alignment and phylogenetic analysis was conducted. Then for further study the crystal structure of the PeRP protein, the recombinant expression pe-SUMO vectors of PeRP were constructed and the protein was expressed in E. coli and purified by nickle beads column and size column. Results showed that the PeRP gene contained a 1.275 kb open reading frame (ORF) coding a 425 amino acid polypeptide, which contained the typical domain of UDF299 and was predicted as a number of kinase-PPPase superfamily. The multiple sequence alignment and phylogenetic analysis of PeRP revealed that Phyllostachys edulis was a typical C3 monocotyledon. Expressed soluble PeRP1 protein had three forms--polymer, dimmers, and monomers in water soultion. These provided a foundation for the structure and function of RP.[Ch, 7 fig. 15 ref.]

WANG Chaoli, ZHANG Zhijun, QU Yaping, WANG Lei. Cloning, expression and purification of pyruvate, orthophosphate dikinase regulatory proteins from Phyllostachys edulis[J]. Journal of Zhejiang A&F University, 2015, 32(5): 749-755. doi: 10.11833/j.issn.2095-0756.2015.05.014
Citation: WANG Chaoli, ZHANG Zhijun, QU Yaping, WANG Lei. Cloning, expression and purification of pyruvate, orthophosphate dikinase regulatory proteins from Phyllostachys edulis[J]. Journal of Zhejiang A&F University, 2015, 32(5): 749-755. doi: 10.11833/j.issn.2095-0756.2015.05.014

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