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26 results on '"Dan, Jiameng"'

1. List of contributors

Author

Altucci, Lucia, primary, Alvarez, Rosana, additional, Aprile, Marianna, additional, Asmar, Fazila, additional, Atasoylu, Onur, additional, Bailey-Whyte, Maeve, additional, Baird, Anne-Marie, additional, Banila, Cristiana, additional, Barkey, Natalie, additional, Bayeva, Nadiya, additional, Blanquart, Christophe, additional, Cerchietti, Leandro, additional, Chen, Taiping, additional, Cinque, Sonia, additional, Connolly, Roisin M., additional, Conroy, Michael, additional, Cosgrave, Joanne M., additional, Costa, Valerio, additional, Dan, Jiameng, additional, de Lera, Angel R., additional, Dhanak, Dashyant, additional, Digby, Barry, additional, Dowling, Catríona M., additional, Ennis, Sarah, additional, Franklin, Kierra A., additional, Gillberg, Linn, additional, Gray, Steven G., additional, Greenfield, Graeme, additional, Greenleaf, William J., additional, Grønbæk, Kirsten, additional, Haynes, Karmella A., additional, Ilieva, Mirolyuba, additional, Kauppinen, Sakari, additional, Kaypee, Stephanie, additional, Keenan, Catherine E., additional, Kelleher, Robbie, additional, Kim, Samuel H., additional, Kim, Sunkyu, additional, King, Ellen, additional, Kirschner, Michaela B., additional, Kundu, Tapas K., additional, Leucci, Eleonora, additional, Martella, Andrea, additional, Metzl-Raz, Eyal, additional, Mills, Ken I., additional, Mohd-Sarip, Adone, additional, Moody, Hannah L., additional, Nebbioso, Angela, additional, Ó Broin, Pilib, additional, Orumaa, Kristen, additional, O’Connor, Áine, additional, Pauklin, Siim, additional, Perry, Antoinette S., additional, Piskareva, Olga, additional, Pook, Hannah, additional, Preston, Patrick, additional, Revuelta, Maria, additional, Roussos Torres, Evanthia T., additional, Sian, Veronica, additional, Singh, Siddharth, additional, Souto, José A., additional, Stallings, Raymond L., additional, Swarnkar, Sumedha, additional, Uchida, Shizuka, additional, Venney, Deirdra, additional, Walker, Harriet R., additional, Zhang, Catherine R., additional, and Zheng, Shijie C., additional

Published
2023
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3. Genetic Studies on Mammalian DNA Methyltransferases

Author

Dan, Jiameng, Chen, Taiping, Crusio, Wim E., Series Editor, Dong, Haidong, Series Editor, Radeke, Heinfried H., Series Editor, Rezaei, Nima, Series Editor, Steinlein, Ortrud, Series Editor, Xiao, Junjie, Series Editor, Jeltsch, Albert, editor, and Jurkowska, Renata Z., editor

Published
2022
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14. Roles for Histone Acetylation in Regulation of Telomere Elongation and Two-cell State in Mouse ES Cells

Author

Dan, Jiameng, Yang, Jiao, Liu, Yifei, Xiao, Andrew, and Liu, Lin

Subjects
Histones, Mice, Animals, RNA, Acetylation, DNA Methylation, Telomere, Telomerase, Article, Embryonic Stem Cells, Epigenesis, Genetic, Histone Acetyltransferases
Abstract

Mammalian telomeres and subtelomeres are marked by heterochromatic epigenetic modifications, including repressive DNA methylation and histone methylation (e.g., H3K9me3 and H4K20me3). Loss of these epigenetic marks results in increased rates of telomere recombination and elongation. Other than these repressive epigenetic marks, telomeric and subtelomeric H3 and H4 are underacetylated. Yet, whether histone acetylation also regulates telomere length has not been directly addressed. We thought to test the effects of histone acetylation levels on telomere length using histone deacetylase (HDAC) inhibitor (sodium butyrate, NaB) that mediates histone hyperacetylation and histone acetyltransferase (HAT) inhibitor (C646) that mediates histone hypoacetylation. We show that histone hyperacetylation dramatically elongates telomeres in wild-type ES cells, and only slightly elongates telomeres in Terc(-/-) ES cells, suggesting that Terc is involved in histone acetylation-induced telomere elongation. In contrast, histone hypoacetylation shortens telomeres in both wild-type and Terc(-/-) ES cells. Additionally, histone hyperacetylation activates 2-cell (2C) specific genes including Zscan4, which is involved in telomere recombination and elongation, whereas histone hypoacetylation represses Zscan4 and 2C genes. These data suggest that histone acetylation levels affect the heterochromatic state at telomeres and subtelomeres, and regulate gene expression at subtelomeres, linking histone acetylation to telomere length maintenance.

Published
2015

15. Tet Enzymes Regulate Telomere Maintenance and Chromosomal Stability of Mouse ESCs

Author

Yang, Jiao, primary, Guo, Renpeng, additional, Wang, Hua, additional, Ye, Xiaoying, additional, Zhou, Zhongcheng, additional, Dan, Jiameng, additional, Wang, Haiying, additional, Gong, Peng, additional, Deng, Wei, additional, Yin, Yu, additional, Mao, ShiQing, additional, Wang, Lingbo, additional, Ding, Junjun, additional, Li, Jinsong, additional, Keefe, David L., additional, Dawlaty, Meelad M., additional, Wang, Jianlong, additional, Xu, GuoLiang, additional, and Liu, Lin, additional

Published
2016
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20. Rif1 Maintains Telomere Length Homeostasis of ESCs by Mediating Heterochromatin Silencing

Author

Dan, Jiameng, primary, Liu, Yifei, additional, Liu, Na, additional, Chiourea, Maria, additional, Okuka, Maja, additional, Wu, Tao, additional, Ye, Xiaoying, additional, Mou, Chunlin, additional, Wang, Lei, additional, Wang, Lingling, additional, Yin, Yu, additional, Yuan, Jihong, additional, Zuo, Bingfeng, additional, Wang, Fang, additional, Li, Zhiguo, additional, Pan, Xinghua, additional, Yin, Zhinan, additional, Chen, Lingyi, additional, Keefe, David L., additional, Gagos, Sarantis, additional, Xiao, Andrew, additional, and Liu, Lin, additional

Published
2014
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23. Molecular insights into the heterogeneity of telomere reprogramming in induced pluripotent stem cells

Author

Wang, Fang, primary, Yin, Yu, additional, Ye, Xiaoying, additional, Liu, Kai, additional, Zhu, Haiying, additional, Wang, Lingling, additional, Chiourea, Maria, additional, Okuka, Maja, additional, Ji, Guangzhen, additional, Dan, Jiameng, additional, Zuo, Bingfeng, additional, Li, Minshu, additional, Zhang, Qian, additional, Liu, Na, additional, Chen, Lingyi, additional, Pan, Xinghua, additional, Gagos, Sarantis, additional, Keefe, David L, additional, and Liu, Lin, additional

Published
2011
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24. Molecular insights into the heterogeneity of telomere reprogramming in induced pluripotent stem cells.

Author

Wang, Fang, Yin, Yu, Ye, Xiaoying, Liu, Kai, Zhu, Haiying, Wang, Lingling, Chiourea, Maria, Okuka, Maja, Ji, Guangzhen, Dan, Jiameng, Zuo, Bingfeng, Li, Minshu, Zhang, Qian, Liu, Na, Chen, Lingyi, Pan, Xinghua, Gagos, Sarantis, Keefe, David L, and Liu, Lin

Subjects
REJUVENATION, INDUCED pluripotent stem cells, TELOMERES, ELONGATION factors (Biochemistry), EMBRYONIC stem cells, HETEROGENEITY
Abstract

Rejuvenation of telomeres with various lengths has been found in induced pluripotent stem cells (iPSCs). Mechanisms of telomere length regulation during induction and proliferation of iPSCs remain elusive. We show that telomere dynamics are variable in mouse iPSCs during reprogramming and passage, and suggest that these differences likely result from multiple potential factors, including the telomerase machinery, telomerase-independent mechanisms and clonal influences including reexpression of exogenous reprogramming factors. Using a genetic model of telomerase-deficient (Terc−/− and Terc+/−) cells for derivation and passages of iPSCs, we found that telomerase plays a critical role in reprogramming and self-renewal of iPSCs. Further, telomerase maintenance of telomeres is necessary for induction of true pluripotency while the alternative pathway of elongation and maintenance by recombination is also required, but not sufficient. Together, several aspects of telomere biology may account for the variable telomere dynamics in iPSCs. Notably, the mechanisms employed to maintain telomeres during iPSC reprogramming are very similar to those of embryonic stem cells. These findings may also relate to the cloning field where these mechanisms could be responsible for telomere heterogeneity after nuclear reprogramming by somatic cell nuclear transfer. [ABSTRACT FROM AUTHOR]

Published
2012
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25. The ICF syndrome protein CDCA7 harbors a unique DNA binding domain that recognizes a CpG dyad in the context of a non-B DNA.

Author

Hardikar S, Ren R, Ying Z, Zhou J, Horton JR, Bramble MD, Liu B, Lu Y, Liu B, Coletta LD, Shen J, Dan J, Zhang X, Cheng X, and Chen T

Subjects
Humans, DNA-Binding Proteins metabolism, DNA-Binding Proteins genetics, DNA-Binding Proteins chemistry, Protein Domains, DNA metabolism, Cell Cycle Proteins metabolism, Cell Cycle Proteins genetics, Cell Cycle Proteins chemistry, Mutation, Heterochromatin metabolism, Heterochromatin genetics, Face abnormalities, Nuclear Proteins, Primary Immunodeficiency Diseases metabolism, Primary Immunodeficiency Diseases genetics, DNA Methylation, CpG Islands, Protein Binding, Immunologic Deficiency Syndromes metabolism, Immunologic Deficiency Syndromes genetics, Centromere metabolism
Abstract

CDCA7 , encoding a protein with a carboxyl-terminal cysteine-rich domain (CRD), is mutated in immunodeficiency, centromeric instability, and facial anomalies (ICF) syndrome, a disease related to hypomethylation of juxtacentromeric satellite DNA. How CDCA7 directs DNA methylation to juxtacentromeric regions is unknown. Here, we show that the CDCA7 CRD adopts a unique zinc-binding structure that recognizes a CpG dyad in a non-B DNA formed by two sequence motifs. CDCA7, but not ICF mutants, preferentially binds the non-B DNA with strand-specific CpG hemi-methylation. The unmethylated sequence motif is highly enriched at centromeres of human chromosomes, whereas the methylated motif is distributed throughout the genome. At S phase, CDCA7, but not ICF mutants, is concentrated in constitutive heterochromatin foci, and the formation of such foci can be inhibited by exogenous hemi-methylated non-B DNA bound by the CRD. Binding of the non-B DNA formed in juxtacentromeric regions during DNA replication provides a mechanism by which CDCA7 controls the specificity of DNA methylation.

Published
2024
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26. The ICF syndrome protein CDCA7 harbors a unique DNA-binding domain that recognizes a CpG dyad in the context of a non-B DNA.

Author

Hardikar S, Ren R, Ying Z, Horton JR, Bramble MD, Liu B, Lu Y, Liu B, Dan J, Zhang X, Cheng X, and Chen T

Abstract

CDCA7 , encoding a protein with a C-terminal cysteine-rich domain (CRD), is mutated in immunodeficiency, centromeric instability and facial anomalies (ICF) syndrome, a disease related to hypomethylation of juxtacentromeric satellite DNA. How CDCA7 directs DNA methylation to juxtacentromeric regions is unknown. Here, we show that the CDCA7 CRD adopts a unique zinc-binding structure that recognizes a CpG dyad in a non-B DNA formed by two sequence motifs. CDCA7, but not ICF mutants, preferentially binds the non-B DNA with strand-specific CpG hemi-methylation. The unmethylated sequence motif is highly enriched at centromeres of human chromosomes, whereas the methylated motif is distributed throughout the genome. At S phase, CDCA7, but not ICF mutants, is concentrated in constitutive heterochromatin foci, and the formation of such foci can be inhibited by exogenous hemi-methylated non-B DNA bound by the CRD. Binding of the non-B DNA formed in juxtacentromeric regions during DNA replication provides a mechanism by which CDCA7 controls the specificity of DNA methylation.

Published
2023
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