Isolation and expression analysis of a GDSL-like lipase gene from Brassica napus L.

被引:3
作者
Ling, Hua
Zhao, Jingya
Zuo, Kaijing
Qiu, Chengxiang
Yao, Hongyan
Qin, Jie
Sun, Xiaofen
Tang, Kexuan [1 ]
机构
[1] Shanghai Jiao Tong Univ, Plant Biotechnol Res Ctr, Fudan SJTU Nottingham Plant Biotechnol R&D Ctr, Sch Agr & Biol,Sch Life Sci & Technol,Shanghai Ke, Shanghai 200030, Peoples R China
[2] Fudan Univ, Fudan SJTU Nottingham Plant Biotechnol R&D Ctr, Morgan Tan Int Ctr Life Sci, Shanghai 200433, Peoples R China
来源
JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY | 2006年 / 39卷 / 03期
关键词
Brassica napus; GDSL lipase; RACE; root-deficient; RT-PCR;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
As lipolytic enzymes, GDSL lipases play an important role in plant growth and development. In order to identify their functions and roles, the full-length cDNA of a GDSL lipase gene, designated BnLIP2, was isolated from Brassica napus L. BnLIP2 was 1,300 bp long, with 1,122 bp open reading frame (ORF) encoding 373 amino acid residues. Sequence analysis indicated that BnLIP2 belonged to GDSL family. Southern blot analysis indicated that BnLIP2 belonged to a small gene family in rapeseed genome. RT-PCR analysis revealed that BnLIP2 was a tissue-specific expressing gene during reproductive growth and strongly expressed during seed germination. BnLIP2 expression could not be detected until three days after germination, and it subsequently became stronger. The transcript of this gene was deficient in root of seedlings growing at different stages. When juvenile seedlings were treated by methyl jasmonate (MeJ), salicylic acid (SA) and naphthalene acetic acid (NAA), BnLIP2 expression could not be induced in root. Our study implicates that BnLIP2 probably plays an important role in rapeseed germination, morphogenesis, flowering, but independent of root growth and development.
引用
收藏
页码:297 / 303
页数:7
相关论文
共 25 条
[11]   The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates [J].
Lee, YL ;
Chen, JC ;
Shaw, JF .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1997, 231 (02) :452-456
[12]   C-terminal His-tagging results in substrate specificity changes of the thioesterase I from Escherichia coli [J].
Lee, YL ;
Su, MS ;
Huang, TH ;
Shaw, JF .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 1999, 76 (10) :1113-1118
[13]  
Li J, 2000, NAT STRUCT BIOL, V7, P555
[14]   Crystallization and preliminary X-ray crystallographic analysis of thioesterase I from Escherichia coli [J].
Lo, YC ;
Lee, YL ;
Shaw, JF ;
Liaw, YC .
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2000, 56 :756-757
[15]   Gene families from the Arabidopsis thaliana pollen coat proteome [J].
Mayfield, JA ;
Fiebig, A ;
Johnstone, SE ;
Preuss, D .
SCIENCE, 2001, 292 (5526) :2482-2485
[16]   Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases [J].
Molgaard, A ;
Kauppinen, S ;
Larsen, S .
STRUCTURE, 2000, 8 (04) :373-383
[17]   Secretome analysis reveals an Arabidopsis lipase involved in defense against Alternaria brassicicola [J].
Oh, IS ;
Park, AR ;
Bae, MS ;
Kwon, SJ ;
Kim, YS ;
Lee, JE ;
Kang, NY ;
Lee, SM ;
Cheong, H ;
Park, OK .
PLANT CELL, 2005, 17 (10) :2832-2847
[18]   Purification of ENOD8 proteins from Medicago sativa root nodules and their characterization as esterases [J].
Pringle, D ;
Dickstein, R .
PLANT PHYSIOLOGY AND BIOCHEMISTRY, 2004, 42 (01) :73-79
[19]   Identification and characterization of a GDSL esterase gene located proximal to the swr quorum-sensing system of Serratia liquefaciens MG1 [J].
Riedel, K ;
Talker-Huiber, D ;
Givskov, M ;
Schwab, H ;
Eberl, L .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2003, 69 (07) :3901-3910
[20]   Functional expression of an ajmaline pathway-specific esterase from Rauvolfia in a novel plant-virus expression system [J].
Ruppert, M ;
Woll, J ;
Giritch, A ;
Genady, E ;
Ma, XY ;
Stöckigt, J .
PLANTA, 2005, 222 (05) :888-898