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Gong Xiaowei,Luo Huajun,Hong Liu,Wu Jun,Wu Heng,Song Chunxia,Zhao Wei,Han Yi,Dao Ya,Zhang Xia,Zhu Donglai,Luo Yiyong 한국미생물학회 2022 The journal of microbiology Vol.60 No.8
Tryptophol (TOL) is a metabolic derivative of tryptophan (Trp) and shows pleiotropic effects in humans, plants and microbes. In this study, the effect of Trp and phenylalanine (Phe) on TOL production in Saccharomyces cerevisiae was determined, and a systematic interpretation of TOL accumulation was offered by transcriptomic and metabolomic analyses. Trp significantly promoted TOL production, but the output plateaued (231.02−266.31 mg/L) at Trp concentrations ≥ 0.6 g/L. In contrast, Phe reduced the stimulatory effect of Trp, which was strongly dependent on the Phe concentration. An integrated genomic, transcriptomic, and metabolomic analysis revealed that the effect of Trp and Phe on TOL production was mainly related to the transamination and decarboxylation of the Ehrlich pathway. Additionally, other genes, including thiamine regulon genes (this), the allantoin catabolic genes dal1, dal2, dal4, and the transcriptional activator gene aro80, may play important roles. These findings were partly supported by the fact that the thi4 gene was involved in TOL production, as shown by heterologous expression analysis. To the best of our knowledge, this novel biological function of thi4 in S. cerevisiae is reported here for the first time. Overall, our findings provide insights into the mechanism of TOL production, which will contribute to TOL production using metabolic engineering strategies.
Zhang, Yan-Li,Li, Qing,Yang, Xiao-Mei,Fang, Fang,Li, Jun,Wang, Ya-Hui,Yang, Qin,Zhu, Lei,Nie, Hui-Zhen,Zhang, Xue-Li,Feng, Ming-Xuan,Jiang, Shu-Heng,Tian, Guang-Ang,Hu, Li-Peng,Lee, Ho-Young,Lee, Su-J American Association for Cancer Research 2018 Cancer research Vol.78 No.9
<P>Matricellular protein SPON2 acts as an HCC suppressor and utilizes distinct signaling events to perform dual functions in HCC microenvironment.</P><P>Tumor-associated macrophages (TAM) represent key regulators of the complex interplay between cancer and the immune microenvironment. Matricellular protein SPON2 is essential for recruiting lymphocytes and initiating immune responses. Recent studies have shown that SPON2 has complicated roles in cell migration and tumor progression. Here we report that, in the tumor microenvironment of hepatocellular carcinoma (HCC), SPON2 not only promotes infiltration of M1-like macrophages but also inhibits tumor metastasis. SPON2-α4β1 integrin signaling activated RhoA and Rac1, increased F-actin reorganization, and promoted M1-like macrophage recruitment. F-Actin accumulation also activated the Hippo pathway by suppressing LATS1 phosphorylation, promoting YAP nuclear translocation, and initiating downstream gene expression. However, SPON2-α5β1 integrin signaling inactivated RhoA and prevented F-actin assembly, thereby inhibiting HCC cell migration; the Hippo pathway was not noticeably involved in SPON2-mediated HCC cell migration. In HCC patients, SPON2 levels correlated positively with prognosis. Overall, our findings provide evidence that SPON2 is a critical factor in mediating the immune response against tumor cell growth and migration in HCC.</P><P><B>Significance:</B> Matricellular protein SPON2 acts as an HCC suppressor and utilizes distinct signaling events to perform dual functions in HCC microenvironment.</P><P><B>Graphical Abstract:</B> http://cancerres.aacrjournals.org/content/canres/78/9/2305/F1.large.jpg. <I>Cancer Res; 78(9); 2305–17. ©2018 AACR</I>.</P><P><B>Graphical Abstract</B></P><P> [Figure]</P>
Protein Microarray Characterization of the <i>S</i> -Nitrosoproteome
Lee, Yun-Il,Giovinazzo, Daniel,Kang, Ho Chul,Lee, Yunjong,Jeong, Jun Seop,Doulias, Paschalis-Thomas,Xie, Zhi,Hu, Jianfei,Ghasemi, Mehdi,Ischiropoulos, Harry,Qian, Jiang,Zhu, Heng,Blackshaw, Seth,Dawso The American Society for Biochemistry and Molecula 2014 Molecular and Cellular Proteomics Vol.13 No.1
<P>Nitric oxide (NO) mediates a substantial part of its physiologic functions via <I>S</I>-nitrosylation, however the cellular substrates for NO-mediated <I>S</I>-nitrosylation are largely unknown. Here we describe the <I>S</I>-nitrosoproteome using a high-density protein microarray chip containing 16,368 unique human proteins. We identified 834 potentially <I>S</I>-nitrosylated human proteins. Using a unique and highly specific labeling and affinity capture of <I>S</I>-nitrosylated proteins, 138 cysteine residues on 131 peptides in 95 proteins were determined, defining critical sites of NO's actions. Of these cysteine residues 113 are novel sites of <I>S</I>-nitrosylation. A consensus sequence motif from these 834 proteins for <I>S</I>-nitrosylation was identified, suggesting that the residues flanking the <I>S</I>-nitrosylated cysteine are likely to be the critical determinant of whether the cysteine is <I>S</I>-nitrosylated. We identify eight ubiquitin E3 ligases, RNF10, RNF11, RNF41, RNF141, RNF181, RNF208, WWP2, and UBE3A, whose activities are modulated by <I>S</I>-nitrosylation, providing a unique regulatory mechanism of the ubiquitin proteasome system. These results define a new and extensive set of proteins that are susceptible to NO regulation via <I>S</I>-nitrosylation. Similar approaches could be used to identify other post-translational modification proteomes.</P>