Functional divergence of betaine aldehyde dehydrogenase genes in Populus euphratica.
- Author:
Jiaqi LIU
1
;
Xue YANG
;
Li DI
;
Hailing YANG
Author Information
1. College of Life Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China.
- Publication Type:Journal Article
- MeSH:
Amino Acid Sequence;
Betaine-Aldehyde Dehydrogenase;
biosynthesis;
genetics;
Cloning, Molecular;
Escherichia coli;
genetics;
metabolism;
Gene Expression Regulation, Plant;
physiology;
Molecular Sequence Data;
Plant Proteins;
biosynthesis;
chemistry;
genetics;
Populus;
genetics;
Protein Isoforms;
chemistry;
metabolism;
Recombinant Proteins;
biosynthesis;
genetics;
isolation & purification;
Substrate Specificity
- From:
Chinese Journal of Biotechnology
2012;28(3):329-339
- CountryChina
- Language:Chinese
-
Abstract:
Plant betaine aldehyde dehydrogenase (BADH) is a physiologically important enzyme in response to salt or drought stress. In this study, two BADH genes (PeBADH1 and PeBADH2) were cloned from Populus euphratica. Both PeBADH1 and PeBADH2 genes encode the proteins of 503 amino acid residues, with a calculated molecular mass of 54.93 kDa and 54.90 kDa, respectively. Reverse transcription PCR showed the divergence of expression pattern between the PeBADH1 and PeBADH2 genes in P. euphratica. The recombinant PeBADH1 and PeBADH2 proteins were overexpressed in E. coli, and purified by Ni-affinity chromatography. The PeBADH2 protein had 1.5-fold higher enzymatic activity towards the substrate aldehyde than PeBADH1 protein. The PeBADH1 protein revealed higher thermal stability than PeBADH2 protein. These results indicated obvious functional divergence between the PeBADH1 and PeBADH2 genes.
