Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos

Publication Date:
2018-08-23
Publisher:
American Association for the Advancement of Science (AAAS)
Electronic ISSN:
2375-2548
Topics:
Natural Sciences in General
Published by:
http://www.aaas.org/
_version_ 1836399035327447040
autor Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
beschreibung Heterochromatin formation during early embryogenesis is timed precisely, but how this process is regulated remains elusive. We report the discovery of a histone methyltransferase complex whose nuclear accumulation and activation establish the onset of heterochromatin formation in Caenorhabditis elegans embryos. We find that the inception of heterochromatin generation coincides with the accumulation of the histone H3 lysine 9 (H3K9) methyltransferase MET-2 (SETDB) into nuclear hubs. The absence of MET-2 results in delayed and disturbed heterochromatin formation, whereas accelerated nuclear localization of the methyltransferase leads to precocious H3K9 methylation. We identify two factors that bind to and function with MET-2: LIN-65, which resembles activating transcription factor 7–interacting protein (ATF7IP) and localizes MET-2 into nuclear hubs, and ARLE-14, which is orthologous to adenosine 5'-diphosphate–ribosylation factor-like 14 effector protein (ARL14EP) and promotes stable association of MET-2 with chromatin. These data reveal that nuclear accumulation of MET-2 in conjunction with LIN-65 and ARLE-14 regulates timing of heterochromatin domains during embryogenesis.
citation_standardnr 6323000
datenlieferant ipn_articles
feed_id 228416
feed_publisher American Association for the Advancement of Science (AAAS)
feed_publisher_url http://www.aaas.org/
insertion_date 2018-08-23
journaleissn 2375-2548
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher American Association for the Advancement of Science (AAAS)
quelle Science Advances
relation http://advances.sciencemag.org/cgi/content/short/4/8/eaat6224?rss=1
search_space articles
shingle_author_1 Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
shingle_author_2 Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
shingle_author_3 Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
shingle_author_4 Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
shingle_catch_all_1 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
Heterochromatin formation during early embryogenesis is timed precisely, but how this process is regulated remains elusive. We report the discovery of a histone methyltransferase complex whose nuclear accumulation and activation establish the onset of heterochromatin formation in Caenorhabditis elegans embryos. We find that the inception of heterochromatin generation coincides with the accumulation of the histone H3 lysine 9 (H3K9) methyltransferase MET-2 (SETDB) into nuclear hubs. The absence of MET-2 results in delayed and disturbed heterochromatin formation, whereas accelerated nuclear localization of the methyltransferase leads to precocious H3K9 methylation. We identify two factors that bind to and function with MET-2: LIN-65, which resembles activating transcription factor 7–interacting protein (ATF7IP) and localizes MET-2 into nuclear hubs, and ARLE-14, which is orthologous to adenosine 5'-diphosphate–ribosylation factor-like 14 effector protein (ARL14EP) and promotes stable association of MET-2 with chromatin. These data reveal that nuclear accumulation of MET-2 in conjunction with LIN-65 and ARLE-14 regulates timing of heterochromatin domains during embryogenesis.
Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
American Association for the Advancement of Science (AAAS)
2375-2548
23752548
shingle_catch_all_2 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
Heterochromatin formation during early embryogenesis is timed precisely, but how this process is regulated remains elusive. We report the discovery of a histone methyltransferase complex whose nuclear accumulation and activation establish the onset of heterochromatin formation in Caenorhabditis elegans embryos. We find that the inception of heterochromatin generation coincides with the accumulation of the histone H3 lysine 9 (H3K9) methyltransferase MET-2 (SETDB) into nuclear hubs. The absence of MET-2 results in delayed and disturbed heterochromatin formation, whereas accelerated nuclear localization of the methyltransferase leads to precocious H3K9 methylation. We identify two factors that bind to and function with MET-2: LIN-65, which resembles activating transcription factor 7–interacting protein (ATF7IP) and localizes MET-2 into nuclear hubs, and ARLE-14, which is orthologous to adenosine 5'-diphosphate–ribosylation factor-like 14 effector protein (ARL14EP) and promotes stable association of MET-2 with chromatin. These data reveal that nuclear accumulation of MET-2 in conjunction with LIN-65 and ARLE-14 regulates timing of heterochromatin domains during embryogenesis.
Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
American Association for the Advancement of Science (AAAS)
2375-2548
23752548
shingle_catch_all_3 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
Heterochromatin formation during early embryogenesis is timed precisely, but how this process is regulated remains elusive. We report the discovery of a histone methyltransferase complex whose nuclear accumulation and activation establish the onset of heterochromatin formation in Caenorhabditis elegans embryos. We find that the inception of heterochromatin generation coincides with the accumulation of the histone H3 lysine 9 (H3K9) methyltransferase MET-2 (SETDB) into nuclear hubs. The absence of MET-2 results in delayed and disturbed heterochromatin formation, whereas accelerated nuclear localization of the methyltransferase leads to precocious H3K9 methylation. We identify two factors that bind to and function with MET-2: LIN-65, which resembles activating transcription factor 7–interacting protein (ATF7IP) and localizes MET-2 into nuclear hubs, and ARLE-14, which is orthologous to adenosine 5'-diphosphate–ribosylation factor-like 14 effector protein (ARL14EP) and promotes stable association of MET-2 with chromatin. These data reveal that nuclear accumulation of MET-2 in conjunction with LIN-65 and ARLE-14 regulates timing of heterochromatin domains during embryogenesis.
Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
American Association for the Advancement of Science (AAAS)
2375-2548
23752548
shingle_catch_all_4 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
Heterochromatin formation during early embryogenesis is timed precisely, but how this process is regulated remains elusive. We report the discovery of a histone methyltransferase complex whose nuclear accumulation and activation establish the onset of heterochromatin formation in Caenorhabditis elegans embryos. We find that the inception of heterochromatin generation coincides with the accumulation of the histone H3 lysine 9 (H3K9) methyltransferase MET-2 (SETDB) into nuclear hubs. The absence of MET-2 results in delayed and disturbed heterochromatin formation, whereas accelerated nuclear localization of the methyltransferase leads to precocious H3K9 methylation. We identify two factors that bind to and function with MET-2: LIN-65, which resembles activating transcription factor 7–interacting protein (ATF7IP) and localizes MET-2 into nuclear hubs, and ARLE-14, which is orthologous to adenosine 5'-diphosphate–ribosylation factor-like 14 effector protein (ARL14EP) and promotes stable association of MET-2 with chromatin. These data reveal that nuclear accumulation of MET-2 in conjunction with LIN-65 and ARLE-14 regulates timing of heterochromatin domains during embryogenesis.
Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler-Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., Mango, S. E.
American Association for the Advancement of Science (AAAS)
2375-2548
23752548
shingle_title_1 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
shingle_title_2 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
shingle_title_3 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
shingle_title_4 Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
timestamp 2025-06-30T23:36:34.640Z
titel Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
titel_suche Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos
topic TA-TD
uid ipn_articles_6323000