Sheng-Li Tian

Shenzhen University, Shenzhen, Guangdong Sheng, China

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Publications (4)5.75 Total impact

  • Shenzhen Daxue Xuebao (Ligong Ban)/Journal of Shenzhen University Science and Engineering 12/2012; 29(6):521-526. DOI:10.3724/SP.J.1249.2012.06521
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    ABSTRACT: Ribonucleic acid interference (RNAi) inhibits the expression of target genes in a sequence-specific manner, and shows potential for gene knockdown in filamentous fungi, in which the locus-specific gene knockout occurs in low frequency. In this study, the function of the repressor of cellulase expression I (ACEI) was verified in Trichoderma koningii (T. koningii) YC01 through RNAi, and ace1- silenced strains with improved cellulase productivity were obtained. An expression cassette that transcribed the interfering double-stranded RNA (dsRNA) of ace1 was constructed and transformed into T. koningii, and the transformants, in which the expression of ace1 was successfully silenced, were selected. As a result of the ace1 gene silencing, the expression levels of the main cellulase and xylanase genes were elevated, and the enhanced production of total proteins, cellulase, and xylanase was observed in the cultivation. In addition, the downregulation of ace1 resulted in an increasing expression of xyr1, but no clear variation in the expression of cre1, which suggested that ACEI acted as a repressor of the xyr1 transcription, but was not involved in the regulation of the cre1 expression. The results of this work indicate that ace1 is a valid target gene for enhancing enzyme production in T. koningii, and RNAi is an appropriate tool for improving the properties of industrial fungi.
    Journal of Microbiology and Biotechnology 08/2012; 22(8):1133-40. · 1.32 Impact Factor
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    ABSTRACT: Here, a novel cDNA encoding a serine/arginine (SR)-rich protein, designated PSR, was isolated from the true slime mold Physarum polycephalum and expressed in Escherichia coli. The deduced amino acid (aa) sequence reveals that PSR contains RS repeats at its C-terminus, similar to the conventional PSRPK substrate ASF/SF2. To study the novel protein, we generated a variety of mutant constructs by PCR and site-directed mutagenesis. Our analysis indicated that the purified recombinant PSR was phosphorylated by PSRPK in vitro and the SR-rich domain (amino acids 460-469) in the PSR protein was required for phosphorylation. In addition, removal of the docking motif (amino acids 424-450) from PSR significantly reduced the overall catalytic efficiency of the phosphorylation reaction. We also found that the conserved ATP-binding region (62)LGWGHFSTVWLAIDEKNGGREVALK(86) and the serine/threonine protein kinases active-site signature (184)IIHTDLKPENVLL(196) of PSRPK played a crucial role in substrate phosphorylation and Lys(86) and Asp(188) were crucial for PSRPK phosphorylation of PSR. These results suggest that PSR is a novel SR-related protein that is phosphorylated by PSRPK.
    Journal of Biochemistry 03/2011; 149(3):275-83. DOI:10.1093/jb/mvq141 · 3.07 Impact Factor
  • Gang Liu, Xin Tang, Sheng-Li Tian, Xu Deng, Miao Xing
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    ABSTRACT: The modular structure of the T. reesei endoglucanase IV (EGIV) was reconstructed by fusing EGIV with an additional catalytic module (EGIV-CM). The genes eg4 and eg4-cm were obtained through RT-PCR and gene fusion, and were respectively expressed in recombinant Pichia strains (P. pastoris EGIV1 and P. pastoris EGIV-CM1). The CMC activities of cultivation supernatant of P. pastoris EGIV1 and P. pastoris EGIV-CM1 were 2.4U/ml and 4.3U/ml, respectively. Modification of the EGIV structure with an additional catalytic module improved the specific activity about 4-fold.
    World Journal of Microbiology and Biotechnology 11/2006; 22(12):1301-1305. DOI:10.1007/s11274-006-9176-7 · 1.35 Impact Factor