Page 5 - Molecular Plant Breeding

Molecular Plant Breeding 2011, Vol.2, No.15, 101-108
http://mpb.sophiapublisher.com
101
A Letter Open Access
Bioinformatics Analysis on Ribulose-1,5 -bisphosphate Carboxylase/ Oxygenase
Large Subunits in Different Plants
Biaojin Zhang 1 , Linguang Luo 1 , Xiangxi Zhang 1 , Song Yan 2 , Ruili Li 1 , Dawen Zhang 1 , Yuanyuan
Nie 2 , Yanbing Zeng 1 , Qiegen Liao 1 , Yihua Wei 1
1. Institute of Quality Safety and Standards of Agricultural Products Research, Jiangxi Academy of Agricultural Sciences, Nanchang, 330200, P.R. China
2. Rice Research Institute, Jiangxi Academy of Agricultural Sciences, Nanchang, 330200, P.R. China
Corresponding author email: luolinguang@hotmail.com; Author
Molecular Plant Breeding, 2011, Vol.2 No.15 doi: 10.5376/mpb.2011.02.0015
Received: 29, Sep., 2011
Accepted: 20, Oct., 2011
Published: 26, Jul., 2011
This is an open access article published under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and
reproduction in any medium, provided the original work is properly cited.
Preferred citation for this article:
Zhang et al., 2011, Bioinformatics Analysis on Ribulose-1,5-bisphosphate Carboxylase/ Oxygenase Large Subunits in Different Plants, Molecular Plant
Breeding Vol.2 No.15 (doi: 10.5376/mpb.2011.02.0015)
Abstract Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCo) is a crucial enzyme in plant photosynthesis. Therefore, to
elucidate the characteristics of RuBisCo is important in improving the efficiency of plant photosynthesis, especially the
photosynthetic efficiency in staple crops which relates to the biomass and yield directly. In order to reveal the characters of RuBisCos
from different higher plants, we analyzed the nucleotide sequences and deduced amino acid sequences of ribulose-1,5-bisphosphate
carboxylase/oxygenase large subunits (rbcL) from Zea mays, Arabidopsis thaliana, Pisum sativum, Citrus sinensis, Phalaenopsis
aphrodite subsp. formosana, emphasizing Oryza sativa subsp. Japonica, by the tools of bioinformatics. The sequences data were
collected from the Genbank of National Center for Biotechnology Information (NCBI). The contents of the analysis cover following
aspects: the compositions and the physical and chemical characteristics of nucleotide sequences and deduced amino acid sequences,
signal peptide, transmembrane topological structure, hydrophobicity or hydrophilicity, and secondary structure of the polypeptide,
nucleotide and amino acid sequences comparisons, and molecular systemic evolution of rbcL DNA sequences. As a result, the amino
acid compositions of the rbcLs set out few differentiations. The physical and chemical characteristics are approximately identical
among different higher plants. Signal peptide and transmembrane topological structure were not detected in the rbcLs. We classified
the rbcLs as hydrophilic protein on account of the distributive features of the amino acid residues in the polypeptides. The rbcLs are
mainly composed of α-helix and random coil which are interspersed with extended strand and β-turn elements. The nucleotide
sequences and deduced amino acid sequences possess high homologies among different higher plants. The rbcL DNA sequences can
reflect the evolutionary relationship among various higher plants clearly.
Keywords Ribulose- 1,5- bisphosphate carboxylase/oxygenase (RuBisCo); Plant; Bioinformatics
Background
Ribulose-1,5-bisphosphate carboxylase/oxygenase (EC
4.1.1.39, RuBisCo), transforming the carbon dioxide
and ribulose-1,5-bisphosphate (RuBP) into two
molecular 3-phosphoglyceric acid, catalyzes the first
reaction of carbon dioxide fixation in photosynthetic
dark reaction. Also, RuBisCo catalyzes the reaction of
oxygen and RuBP to phosphoglyceric acid and
phosphoglycollic acid, which is the first reaction of
photorespiration. Therefore, RuBisCo is the key
enzyme deciding the photosynthetic efficiency by
regulating photosynthesis and photorespiration. Base
on the dissimilarity of the primary and quarternary
structures, the RuBisCos can be partitioned into three
types: I form exists in higher plants and most
prokaryotes, consisting of eight large subunits (50~60 kD)
and eight small subunits (12~18 kD), presenting
square symmetry structure (L8S8) (Andersson et al.,
1989); form was discovered in purple nonⅡ -sulfur
photosynthetic bacteria, and composed of only two
large subunits (L 2); form was dug out in
Ⅲ
Thermococcus kodakaracinsis lately by Kitano
(Kitano et al., 2001), likewise formed with only large
subunits, and no small subunit, appearing structure of
(L2)5. The RuBisCo large subunit (rbcL) gene of
higher plants sets in the chloroplast DNA, and it is
translated by chloroplast ribosome. On the contrary,