The Experts below are selected from a list of 324 Experts worldwide ranked by ideXlab platform
Anton M Jetten - One of the best experts on this subject based on the ideXlab platform.
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nabp1 a novel rorγ regulated gene encoding a single stranded Nucleic Acid Binding protein
Biochemical Journal, 2006Co-Authors: Hong Soon Kang, Ju Youn Beak, Robert M Petrovich, Jennifer B Collins, Sherry F Grissom, Anton M JettenAbstract:RORγ2 (retinoid-related orphan receptor γ2) plays a critical role in the regulation of thymopoiesis. Microarray analysis was performed in order to uncover differences in gene expression between thymocytes of wild-type and RORγ−/− mice. This analysis identified a novel gene encoding a 22 kDa protein, referred to as NABP1 (Nucleic-Acid-Binding protein 1). This subsequently led to the identification of an additional protein, closely related to NABP1, designated NABP2. Both proteins contain an OB (oligonucleotide/oligosaccharide Binding) motif at their N-terminus. This motif is highly conserved between the two proteins. NABP1 is highly expressed in the thymus of wild-type mice and is greatly suppressed in RORγ−/− mice. During thymopoiesis, NABP1 mRNA expression is restricted to CD4+CD8+ thymocytes, an expression pattern similar to that observed for RORγ2. These observations appear to suggest that NABP1 expression is regulated either directly or indirectly by RORγ2. Confocal microscopic analysis showed that the NABP1 protein localizes to the nucleus. Analysis of nuclear proteins by size-exclusion chromatography indicated that NABP1 is part of a high molecular-mass protein complex. Since the OB-fold is frequently involved in the recognition of Nucleic Acids, the interaction of NABP1 with various Nucleic Acids was examined. Our results demonstrate that NABP1 binds single-stranded Nucleic Acids, but not double-stranded DNA, suggesting that it functions as a single-stranded Nucleic Acid Binding protein.
Shiping Wang - One of the best experts on this subject based on the ideXlab platform.
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a ccch type zinc finger Nucleic Acid Binding protein quantitatively confers resistance against rice bacterial blight disease
Plant Physiology, 2012Co-Authors: Hanqing Deng, Xianghua Li, Jinghua Xiao, Shiping WangAbstract:Bacterial blight is a devastating disease of rice (Oryza sativa) caused by Xanthomonas oryzae pv oryzae (Xoo). Zinc finger proteins harboring the motif with three conserved cysteine residues and one histidine residue (CCCH) belong to a large family. Although at least 67 CCCH-type zinc finger protein genes have been identified in the rice genome, their functions are poorly understood. Here, we report that one of the rice CCCH-type zinc finger proteins, C3H12, containing five typical CX8-CX5-CX3-H zinc finger motifs, is involved in the rice-Xoo interaction. Activation of C3H12 partially enhanced resistance to Xoo, accompanied by the accumulation of jasmonic Acid (JA) and induced expression of JA signaling genes in rice. In contrast, knockout or suppression of C3H12 resulted in partially increased susceptibility to Xoo, accompanied by decreased levels of JA and expression of JA signaling genes in rice. C3H12 colocalized with a minor disease resistance quantitative trait locus to Xoo, and the enhanced resistance of randomly chosen plants in the quantitative trait locus mapping population correlated with an increased expression level of C3H12. The C3H12 protein localized in the nucleus and possessed Nucleic Acid-Binding activity in vitro. These results suggest that C3H12, as a Nucleic Acid-Binding protein, positively and quantitatively regulates rice resistance to Xoo and that its function is likely associated with the JA-dependent pathway.
Tilmann Burckstummer - One of the best experts on this subject based on the ideXlab platform.
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samhd1 is a Nucleic Acid Binding protein that is mislocalized due to aicardi goutieres syndrome associated mutations
Human Mutation, 2012Co-Authors: Adriana Goncalves, Evren Karayel, Gillian I Rice, Keiryn L Bennett, Yanick J Crow, Giulio Supertifurga, Tilmann BurckstummerAbstract:Aicardi-Gouti�res syndrome (AGS) is a rare inherited autoimmune disease caused by mutations in genes encoding the RNase H2 subunits A, B, and C; the DNase three prime repair exonuclease 1 (TREX1); and sterile alpha motif (SAM) domain and HD domain-containing protein 1 (SAMHD1). Using unbiased affinity purification coupled to protein mass spectrometry, we identify SAMHD1 as a Nucleic-Acid-Binding protein displaying a preference for RNA over DNA. In contrast to TREX1 and the RNase H2 complex, SAMHD1 has no obvious nuclease activity. In addition, interrogating truncation mutants of SAMHD1 observed in AGS patients, we map the Nucleic-Acid-Binding domain to residues 164-442, thus overlapping with the HD domain. Furthermore, we show that although wild-type SAMHD1 displays almost exclusive nuclear localization, 11 of 12 SAMHD1 mutants show at least partial mislocalization to the cytosol. Overall, these data suggest that SAMHD1 has a role in the nucleus that, if disrupted by mutation, leads to cytosolic accumulation of SAMHD1 and autoimmune disease.
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SAMHD1 is a Nucleic‐Acid Binding protein that is mislocalized due to aicardi–goutières syndrome‐associated mutations
Human Mutation, 2012Co-Authors: Adriana Goncalves, Evren Karayel, Gillian I Rice, Keiryn L Bennett, Yanick J Crow, Giulio Superti-furga, Tilmann BurckstummerAbstract:Aicardi-Gouti�res syndrome (AGS) is a rare inherited autoimmune disease caused by mutations in genes encoding the RNase H2 subunits A, B, and C; the DNase three prime repair exonuclease 1 (TREX1); and sterile alpha motif (SAM) domain and HD domain-containing protein 1 (SAMHD1). Using unbiased affinity purification coupled to protein mass spectrometry, we identify SAMHD1 as a Nucleic-Acid-Binding protein displaying a preference for RNA over DNA. In contrast to TREX1 and the RNase H2 complex, SAMHD1 has no obvious nuclease activity. In addition, interrogating truncation mutants of SAMHD1 observed in AGS patients, we map the Nucleic-Acid-Binding domain to residues 164-442, thus overlapping with the HD domain. Furthermore, we show that although wild-type SAMHD1 displays almost exclusive nuclear localization, 11 of 12 SAMHD1 mutants show at least partial mislocalization to the cytosol. Overall, these data suggest that SAMHD1 has a role in the nucleus that, if disrupted by mutation, leads to cytosolic accumulation of SAMHD1 and autoimmune disease.
Hong Soon Kang - One of the best experts on this subject based on the ideXlab platform.
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nabp1 a novel rorγ regulated gene encoding a single stranded Nucleic Acid Binding protein
Biochemical Journal, 2006Co-Authors: Hong Soon Kang, Ju Youn Beak, Robert M Petrovich, Jennifer B Collins, Sherry F Grissom, Anton M JettenAbstract:RORγ2 (retinoid-related orphan receptor γ2) plays a critical role in the regulation of thymopoiesis. Microarray analysis was performed in order to uncover differences in gene expression between thymocytes of wild-type and RORγ−/− mice. This analysis identified a novel gene encoding a 22 kDa protein, referred to as NABP1 (Nucleic-Acid-Binding protein 1). This subsequently led to the identification of an additional protein, closely related to NABP1, designated NABP2. Both proteins contain an OB (oligonucleotide/oligosaccharide Binding) motif at their N-terminus. This motif is highly conserved between the two proteins. NABP1 is highly expressed in the thymus of wild-type mice and is greatly suppressed in RORγ−/− mice. During thymopoiesis, NABP1 mRNA expression is restricted to CD4+CD8+ thymocytes, an expression pattern similar to that observed for RORγ2. These observations appear to suggest that NABP1 expression is regulated either directly or indirectly by RORγ2. Confocal microscopic analysis showed that the NABP1 protein localizes to the nucleus. Analysis of nuclear proteins by size-exclusion chromatography indicated that NABP1 is part of a high molecular-mass protein complex. Since the OB-fold is frequently involved in the recognition of Nucleic Acids, the interaction of NABP1 with various Nucleic Acids was examined. Our results demonstrate that NABP1 binds single-stranded Nucleic Acids, but not double-stranded DNA, suggesting that it functions as a single-stranded Nucleic Acid Binding protein.
Hanqing Deng - One of the best experts on this subject based on the ideXlab platform.
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a ccch type zinc finger Nucleic Acid Binding protein quantitatively confers resistance against rice bacterial blight disease
Plant Physiology, 2012Co-Authors: Hanqing Deng, Xianghua Li, Jinghua Xiao, Shiping WangAbstract:Bacterial blight is a devastating disease of rice (Oryza sativa) caused by Xanthomonas oryzae pv oryzae (Xoo). Zinc finger proteins harboring the motif with three conserved cysteine residues and one histidine residue (CCCH) belong to a large family. Although at least 67 CCCH-type zinc finger protein genes have been identified in the rice genome, their functions are poorly understood. Here, we report that one of the rice CCCH-type zinc finger proteins, C3H12, containing five typical CX8-CX5-CX3-H zinc finger motifs, is involved in the rice-Xoo interaction. Activation of C3H12 partially enhanced resistance to Xoo, accompanied by the accumulation of jasmonic Acid (JA) and induced expression of JA signaling genes in rice. In contrast, knockout or suppression of C3H12 resulted in partially increased susceptibility to Xoo, accompanied by decreased levels of JA and expression of JA signaling genes in rice. C3H12 colocalized with a minor disease resistance quantitative trait locus to Xoo, and the enhanced resistance of randomly chosen plants in the quantitative trait locus mapping population correlated with an increased expression level of C3H12. The C3H12 protein localized in the nucleus and possessed Nucleic Acid-Binding activity in vitro. These results suggest that C3H12, as a Nucleic Acid-Binding protein, positively and quantitatively regulates rice resistance to Xoo and that its function is likely associated with the JA-dependent pathway.
