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Tn5-mutagenesis and identification of atr operon and trpE gene responsible for indole-3-acetic acid synthesis in Azospirillum brasilense Yu62

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Progress in Natural Science:Materials International 2006年第4期16卷 366-372页

作者： xie baoen and chen sanfeng state key laboratory for agrobiotechnology, college of biological sciences, china agricultural university, beijing 100094, china state key laboratory for agrobiotechnology College of Biological Sciences China Agricultural University Beijing 100094 China

To bring more information about synthesis of indole-3-acetic acid (IAA) from Azospirillum brasilense, a Tn5-insertion library of A. brasilense Yu62 was constructed and subjected to screening for IAA producing mutants. Two mutants with decreased IAA levels, named as A3 and A24, were isolated. The sequence analysis of loci tagged showed that the Tn5-1063a was located in the atrA gene encoding GntR family transcriptional regulator and trpE gene encoding component I of anthranilate synthase respectively. At the same time. atrB encoding phosphotransferase and atrC encoding aminotransferase were cloned downstream the atrA gene and atrA, atrB and atrC were clustered in an operon. Mutagenesis and complementation studies showed that atrA and atrC were involved in IAA synthesis. IAA levels of trpE mutant and wild-type strain could be improved by adding anthranilate into the medium.

关键词： indole-3-acetic acid (IAA) IAA mutants Azospirillum brasilense atrABC cluster trpE Tn5 transposon.

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Cloning and sequencing of nifBHDKENX genes of Paenibacillus massiliensis T7 and its nif promoter analysis

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Science china(Life sciences) 2006年第2期49卷 115-122页

作者： ZHAO Hongxin1,2,3, xie baoen2 & chen sanfeng1,2 1. state key laboratory for agrobiotechnology and biological School, china agricultural university, beijing 100094, china 2. key laboratory for Agro-Microbial Resource and Application of Agriculture Ministry, china agricultural university, beijing 100094, china 3. Chemical and biological School, ShenYang Normal university, Shenyang 110034, china 1. state key laboratory for agrobiotechnology and biological School China Agricultural University Beijing 100094 China 2. key laboratory for Agro-Microbial Resource and Application of Agriculture Ministry China Agricultural University Beijing 100094 China 3. Chemical and biological School ShenYang Normal University Shenyang 110034 China

A 324 bp of nifH fragment was PCR amplified from Paenibacillus massiliensis T7 using the universal degenerate primers. The PCR-amplified nifH fragment was labeled with DIG; then used as a probe in Southern blot analysis. Southern blot result showed that there were two positive signals, indicating that there might be two copies of nifH in P. massiliensis T7. A total of 10254 bp DNA sequence containing purD; nifBHDKENX was obtained by five rounds of inverse-PCR amplification. The predicted proteins of nifBHDKENX had high homology with those from other nitrogen-fixing bacteria. Only one putative σ[54]-dependent promoter sequence was detected upstream of the nifB gene; nifBHDKENX were likely to be organized in one operon. Assays of β-galactosidase activity of P. massiliensis T7PB carrying a nifB-lacZ fusion under different concentrations of NH4 [+]; O2 showed that the expression of nifB-lacZ was strongly inhibited by O2.

关键词： Paenibacillus massiliensis T7, nifBHDKENX, nifB-lacZ, inverse-PCR.

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Expression, Characterization and Antimicrobial Ability of a Variant T4 Lysozyme in Pichia pastoris

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agricultural Science & Technology 2014年第3期15卷 321-325页

作者： Ning SUN sanfeng chen Xiangming xie Yueju WANG Gangqiang LI Nan WANG Dehu LIU Biotechnology Research Institute Chinese Academy of Agricultural Sciences key laboratory for agrobiotechnology China Agricultural University Department of Microbiology College of Biological Sciences and Biotechnology Beijing Forestry University Biology Department Macon State College University System of Georgia

T4 lysozyme was engineered with disulfide bonds and expressed in Pichia pastoris. The secreted proteins were purified and made into powder by lyophiliza-tion. Recombinant protein purity was more than 70% measured by HPLC. The lytic activity of variant T4-lysozyme was measured by the lysis of the cel wal of Xan-thomonas oryzae pv. oryzae, X. oryzae pv. oryzicola, Ralstonia solanacearum comb. nov, Clavibacter michiganensis subsp. michiganensis, X. campestris pv. mal-vacearum, Fusarium oxysporium sp. vasinfectum, Verticil ium dahliae kleb. Inhibition zone assay showed that variant T4 lysozyme significantly inhibited X. o. oryzicola and X. c. malvacearum. The antifungal activities of this protein against F. o. vasin-fectum and V. d. kleb were also analyzed.

关键词： Antibacterial activity Expression Pichia pastoris T4 lysozyme Variant

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