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variable requirement for CAF-1 across species might reflect the acquisition of new properties affecting the function of histone H3 variants during evolution of eukaryotes. CAF-1 is essential in mammals but dispensable in Saccharomyces cerevisiae [38]. Interestingly, the budding yeast genome does not contain heterochromatin regions equivalent to those of higher eukaryotes, and several hallmark features of heterochromatin such as di- and trimethylation at H3K9, H3K27, and H4K20 are not observed in the silent chromatin of S. cerevisiae. In mammals, H3K9 dimethylation is predominantly associated with H3.1, but not with H3.3, which carries modifications typically found in transcribed chromatin regions [39]. Outside of the centromeric H3 variant, S. cerevisiae possesses only H3.3, which is expressed and incorporated into chromatin in a replication-independent fashion in higher eukaryotes [12]. These data suggest a specific role for H3.1 in heterochromatin regions. We show here that CAF-1, which is a H3.1 replication-dependent loading complex [11], is specifically required for the nuclear organization of pericentric heterochromatin in embryos and ES cells. One possibility would be a scenario in which incorporation of H3.1 into chromatin is required for the proper nuclear organization of constitutive heterochromatin in an embryonic context. While this has to be addressed experimentally, it is worthwhile to mention an alternate possible mechanism that might explain the disruption of heterochromatin domains in p150CAF-1 null embryos and ES cells. CAF-1 could be required for the loading, into heterochromatin, of an interacting partner required for the clustering of pericentric domains. Following one or two rounds of DNA replication in the absence of p150CAF-1, heterochromatin would become deprived of this molecule, which would cause the disruption of its 3-D organization. A potential candidate is the HP1 protein, which interacts with CAF-1 [13,16]."}

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CAF-1 is essential in mammals but dispensable in Saccharomyces cerevisiae [38]. Interestingly, the budding yeast genome does not contain heterochromatin regions equivalent to those of higher eukaryotes, and several hallmark features of heterochromatin such as di- and trimethylation at H3K9, H3K27, and H4K20 are not observed in the silent chromatin of S. cerevisiae. In mammals, H3K9 dimethylation is predominantly associated with H3.1, but not with H3.3, which carries modifications typically found in transcribed chromatin regions [39]. Outside of the centromeric H3 variant, S. cerevisiae possesses only H3.3, which is expressed and incorporated into chromatin in a replication-independent fashion in higher eukaryotes [12]. These data suggest a specific role for H3.1 in heterochromatin regions. We show here that CAF-1, which is a H3.1 replication-dependent loading complex [11], is specifically required for the nuclear organization of pericentric heterochromatin in embryos and ES cells. One possibility would be a scenario in which incorporation of H3.1 into chromatin is required for the proper nuclear organization of constitutive heterochromatin in an embryonic context. While this has to be addressed experimentally, it is worthwhile to mention an alternate possible mechanism that might explain the disruption of heterochromatin domains in p150CAF-1 null embryos and ES cells. CAF-1 could be required for the loading, into heterochromatin, of an interacting partner required for the clustering of pericentric domains. Following one or two rounds of DNA replication in the absence of p150CAF-1, heterochromatin would become deprived of this molecule, which would cause the disruption of its 3-D organization. A potential candidate is the HP1 protein, which interacts with CAF-1 [13,16]."}

{"project":"2_test","denotations":[{"id":"17083276-9030687-85837839","span":{"begin":251,"end":253},"obj":"9030687"},{"id":"17083276-16267050-85837840","span":{"begin":711,"end":713},"obj":"16267050"},{"id":"17083276-16212490-85837841","span":{"begin":900,"end":902},"obj":"16212490"},{"id":"17083276-14718166-85837842","span":{"begin":1057,"end":1059},"obj":"14718166"},{"id":"17083276-10549285-85837843","span":{"begin":1968,"end":1970},"obj":"10549285"},{"id":"17083276-15306854-85837844","span":{"begin":1971,"end":1973},"obj":"15306854"},{"id":"T48959","span":{"begin":251,"end":253},"obj":"9030687"},{"id":"T40627","span":{"begin":711,"end":713},"obj":"16267050"},{"id":"T76754","span":{"begin":900,"end":902},"obj":"16212490"},{"id":"T49098","span":{"begin":1057,"end":1059},"obj":"14718166"},{"id":"T44850","span":{"begin":1968,"end":1970},"obj":"10549285"},{"id":"T48971","span":{"begin":1971,"end":1973},"obj":"15306854"}],"text":"The variable requirement for CAF-1 across species might reflect the acquisition of new properties affecting the function of histone H3 variants during evolution of eukaryotes. CAF-1 is essential in mammals but dispensable in Saccharomyces cerevisiae [38]. Interestingly, the budding yeast genome does not contain heterochromatin regions equivalent to those of higher eukaryotes, and several hallmark features of heterochromatin such as di- and trimethylation at H3K9, H3K27, and H4K20 are not observed in the silent chromatin of S. cerevisiae. In mammals, H3K9 dimethylation is predominantly associated with H3.1, but not with H3.3, which carries modifications typically found in transcribed chromatin regions [39]. Outside of the centromeric H3 variant, S. cerevisiae possesses only H3.3, which is expressed and incorporated into chromatin in a replication-independent fashion in higher eukaryotes [12]. These data suggest a specific role for H3.1 in heterochromatin regions. We show here that CAF-1, which is a H3.1 replication-dependent loading complex [11], is specifically required for the nuclear organization of pericentric heterochromatin in embryos and ES cells. One possibility would be a scenario in which incorporation of H3.1 into chromatin is required for the proper nuclear organization of constitutive heterochromatin in an embryonic context. While this has to be addressed experimentally, it is worthwhile to mention an alternate possible mechanism that might explain the disruption of heterochromatin domains in p150CAF-1 null embryos and ES cells. CAF-1 could be required for the loading, into heterochromatin, of an interacting partner required for the clustering of pericentric domains. Following one or two rounds of DNA replication in the absence of p150CAF-1, heterochromatin would become deprived of this molecule, which would cause the disruption of its 3-D organization. A potential candidate is the HP1 protein, which interacts with CAF-1 [13,16]."}

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One possibility would be a scenario in which incorporation of H3.1 into chromatin is required for the proper nuclear organization of constitutive heterochromatin in an embryonic context. While this has to be addressed experimentally, it is worthwhile to mention an alternate possible mechanism that might explain the disruption of heterochromatin domains in p150CAF-1 null embryos and ES cells. CAF-1 could be required for the loading, into heterochromatin, of an interacting partner required for the clustering of pericentric domains. Following one or two rounds of DNA replication in the absence of p150CAF-1, heterochromatin would become deprived of this molecule, which would cause the disruption of its 3-D organization. A potential candidate is the HP1 protein, which interacts with CAF-1 [13,16]."}