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Title of Journal: Appl Biochem Biotechnol

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Abbravation: Applied Biochemistry and Biotechnology

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Humana Press Inc

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DOI

10.1007/s10973-012-2921-2

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1559-0291

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Molecular Analysis of OsLEA4 and Its Contributions

Authors: Tingzhang Hu Hua Zeng Shuai He Yingmei Wu Guixue Wang Xiaoyun Huang
Publish Date: 2011/11/06
Volume: 166, Issue: 1, Pages: 222-233
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Abstract

OsLEA4 a late embryogenesis abundant LEA protein gene from rice Oryza sativa L contains a 312bp open reading frame encoding a putative polypeptide of 103 amino acids with a calculated molecular mass of 1119 kDa and a theoretical pI of 1004 OsLEA4 polypeptide is rich in Ala 22 Lys 15 Glu 9 His 8 Thr 8 and Arg 7 and lacking in Trp Cys Asn and Phe residues OsLEA4 protein contains a PfamLEA 1 domain architecture at positions 1–73 with three αhelical domains and without βsheet domain In silico predictions showed that OsLEA4 protein was strongly hydrophilic with the grand average of hydropathy value of −0816 and instability index of 2731 The hydrophilic regions were found in the conserved motif of OsLEA4 OsLEA4 gene was introduced into Escherichia coli and a fusion protein ∼294 kDa was expressed after isopropylthioβdgalactoside inducting by sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis OsLEA4 protein enhanced the tolerance of E coli recombinant to high salinity heat freezing and UV radiation which suggested that OsLEA4 protein may play a protective role under stressed conditions This is the first successful use of E coli as a prokaryotic system for LEA production from riceThis study was supported by the China National Transgenic Major Program 2009ZX08009109B the University Innovation Team Construction Project of Chongqing Education Committee 201040 and The Natural Science Foundation Project of Chongqing Education Committee KJ111108

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