Isolation and Expression Analysis of a GDSL-like Lipase Gene from Brassica napus L.
Open Access
- 31 May 2006
- journal article
- Published by Korean Society for Biochemistry and Molecular Biology - BMB Reports in BMB Reports
- Vol. 39 (3), 297-303
- https://doi.org/10.5483/bmbrep.2006.39.3.297
Abstract
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.Keywords
This publication has 20 references indexed in Scilit:
- GDSL family of serine esterases/lipasesProgress in Lipid Research, 2004
- Purification and cloning of an esterase from the weed black‐grass (Alopecurus myosuroides), which bioactivates aryloxyphenoxypropionate herbicidesThe Plant Journal, 2004
- Isolation and Characterization of the Early Nodule-specific Protein Homologue (Hev b 13), an Allergenic Lipolytic Esterase from Hevea brasiliensis LatexPublished by Elsevier BV ,2004
- Tissue-specific silencing of a transgene in riceProceedings of the National Academy of Sciences of the United States of America, 2002
- C‐terminal His‐tagging results in substrate specificity changes of the thioesterase I from Escherichia coliJournal of Oil & Fat Industries, 1999
- The Thioesterase I ofEscherichia coliHas Arylesterase Activity and Shows Stereospecificity for Protease SubstratesBiochemical and Biophysical Research Communications, 1997
- A new family of lipolytic plant enzymes with members in rice, arabidopsis and maizeFEBS Letters, 1995
- Vibrio mimicus Arylesterase Has Thioesterase and Chymotrypsin-like ActivityBiochemical and Biophysical Research Communications, 1995
- Structure and Function of LipasesAdvances in protein chemistry, 1994
- Crystallization and preliminary X‐ray crystallographic analysis of arylesterase from Pseudomonas fluorescensProteins-Structure Function and Bioinformatics, 1993