Structure of a Novel Rubisco Activase in Gardenia jasminoides
- DOI
- 10.2991/aeecs-18.2018.8How to use a DOI?
- Keywords
- Rubisco; Rubisco activase; Gardenia jasminoides; cDNA library; 3D-structure.
- Abstract
The key photosynthetic CO2-fixing enzyme ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) is regulated by a protein known as Rubisco activase (RCA). RCA is a soluble chloroplast ATPase encoded by nuclear genome that catalyzes the activation of Rubisco in vivo by the ATP-dependent removal of various inhibitory sugar phosphates. In this work, we constructed a G.jasminoides fruit cDNA library, and the GjRCA cDNA was isolated from the library by sequencing method. The GjRCA cDNA contains a predicted 1428 bp open reading frame that encodes 475 amino acids. A bioinformatics analysis was conducted with previously characterized RCAs from other plant species, the results suggested that the GjRCA amino acid sequence has highly conserved nucleotide-binding region, critical ATPase amino acid residue and Rubisco-interaction region with other RCAs. A three-dimensional monomer model of GjRCA was built, GjRCA has extended carboxyl terminus sequence with two conserved cysteine residues, and has 46 kD molecular weight, suggest it's a L-isoform of RCA, it's similar to structure of AAA+ family protein and other RCAs. Conclusion: The results indicated that GjRCA is a L-isofrom RCA of G. jasminoides.
- Copyright
- © 2018, the Authors. Published by Atlantis Press.
- Open Access
- This is an open access article distributed under the CC BY-NC license (http://creativecommons.org/licenses/by-nc/4.0/).
Cite this article
TY - CONF AU - Lan Gao PY - 2018/03 DA - 2018/03 TI - Structure of a Novel Rubisco Activase in Gardenia jasminoides BT - Proceedings of the 2018 2nd International Conference on Advances in Energy, Environment and Chemical Science (AEECS 2018) PB - Atlantis Press SP - 33 EP - 36 SN - 2352-5401 UR - https://doi.org/10.2991/aeecs-18.2018.8 DO - 10.2991/aeecs-18.2018.8 ID - Gao2018/03 ER -