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Ng, Yee ,Ching,Chung, Woo-Chang,Kang, Hye-Ri,Cho, Hye-Jeong,Park, Eun-Byeol,Kang, Suk-Jo,Song, Moon ,Jung Oxford University Press 2018 Nucleic acids research Vol.46 No.17
<P><B>Abstract</B></P><P>DExD/H-box helicase 9 (DHX9), or RNA helicase A (RHA), is an abundant multifunctional nuclear protein. Although it was previously reported to act as a cytosolic DNA sensor in plasmacytoid dendritic cells (pDCs), the role and molecular mechanisms of action of DHX9 in cells that are not pDCs during DNA virus infection are not clear. Here, a macrophage-specific knockout and a fibroblast-specific knockdown of DHX9 impaired antiviral innate immunity against DNA viruses, leading to increased virus replication. DHX9 enhanced NF-κB–mediated transactivation in the nucleus, which required its ATPase-dependent helicase (ATPase/helicase) domain, but not the cytosolic DNA-sensing domain. In addition, DNA virus infection did not induce cytoplasmic translocation of nuclear DHX9 in macrophages and fibroblasts. Nuclear DHX9 was associated with a multiprotein complex including both NF-κB p65 and RNA polymerase II (RNAPII) in chromatin containing NF-κB–binding sites. DHX9 was essential for the recruitment of RNAPII rather than NF-κB p65, to the corresponding promoters; this function also required its ATPase/helicase activity. Taken together, our results show a critical role of nuclear DHX9 (as a transcription coactivator) in the stimulation of NF-κB–mediated innate immunity against DNA virus infection, independently of DHX9’s DNA-sensing function.</P>
Kim, Hoyeun,Na, Sang ,Hyeon,Lee, So-Young,Jeong, Young-Min,Hwang, Hyun-Ju,Hur, Jae ,Young,Park, Sang-Hyun,Woo, Je-Chang,Kim, Sang-Gu Portland Press Ltd. 2012 The Biochemical journal Vol.443 No.1
<P>TDP1 (tyrosyl-DNA phosphodiesterase 1), a member of the PLD (phospholipase D) superfamily, catalyses the hydrolysis of a phosphodiester bond between a tyrosine residue and the 3′-phosphate of DNA. We have previously identified and characterized the <I>AtTDP</I> gene in <I>Arabidopsis thaliana</I>, an orthologue of yeast and human <I>TDP1</I> genes. Sequence alignment of TDP1 orthologues revealed that AtTDP has both a conserved C-terminal TDP domain and, uniquely, an N-terminal SMAD/FHA (forkhead-associated) domain. To help understand the function of this novel enzyme, we analysed the substrate saturation kinetics of full-length AtTDP compared with a truncated AtTDP mutant lacking the N-terminal FHA domain. The recombinant AtTDP protein hydrolysed a single-stranded DNA substrate with <I>K</I><SUB>m</SUB> and <I>k</I><SUB>cat</SUB>/<I>K</I><SUB>m</SUB> values of 703±137 nM and (1.5±0.04)×10<SUP>9</SUP>M<SUP>−1</SUP>·min<SUP>−1</SUP> respectively. The AtTDP-(Δ1–122) protein (TDP domain) showed kinetic parameters that were equivalent to those of the full-length AtTDP protein. A basic amino acid sequence (RKKVKP) within the AtTDP-(Δ123–605) protein (FHA domain) was necessary for nuclear localization of AtTDP. Analysis of active-site mutations showed that a histidine and a lysine residue in each of the HKD motifs were critical for enzyme activity. Vanadates, inhibitors of phosphoryl transfer reactions, inhibited AtTDP enzymatic activity and retarded the growth of an <I>Arabidopsis tdp</I> mutant. Finally, we showed that expression of the <I>AtTDP</I> gene could complement a yeast <I>tdp1</I>Δ<I>rad1</I>Δ mutant, rescuing the growth inhibitory effects of vanadate analogues and CPT (camptothecin). Taken together, the results of the present study demonstrate the structure-based function of AtTDP through which AtTDP can repair DNA strand breaks in plants.</P>
Outcomes of <i>Mycobacterium avium</i> complex lung disease based on clinical phenotype
Koh, Won-Jung,Moon, Seong Mi,Kim, Su-Young,Woo, Min-Ah,Kim, Seonwoo,Jhun, Byung Woo,Park, Hye Yun,Jeon, Kyeongman,Huh, Hee ,Jae,Ki, Chang-Seok,Lee, Nam Yong,Chung, Myung Jin,Lee, Kyung ,Soo,Sh ERS Journals Ltd 2017 The European respiratory journal Vol.50 No.3
<P>Treatment outcomes and redevelopment of NTM lung disease after treatment completion differed by clinical phenotype of MAC lung disease.</P>