The Arabidopsis CSLD5 functions in cell plate formation in a cell cycle dependent manner

Centromere identity is defined by nucleosomes containing CENP-A, a histone H3 variant. The deposition of CENP-A at centromeres is tightly regulated in a cell-cycle-dependent manner. We previously reported that the spatiotemporal control of centromeric CENP-A incorporation is mediated by the phosphorylation of CENP-A Ser68. However, a recent report argued that Ser68 phosphoregulation is dispensable for accurate CENP-A loading. Here, we report that the substitution of Ser68 of endogenous CENP-A with either Gln68 or Glu68 severely impairs CENP-A deposition and cell viability. We also find that mice harboring the corresponding mutations are lethal. Together, these results indicate that the dynamic phosphorylation of Ser68 ensures cell-cycle-dependent CENP-A deposition and cell viability.

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Gcn5-mediated acetylation at MBF-regulated promoters induces the G1/S transcriptional wave

Nucleic Acids Research ◽

10.1093/nar/gkz561 ◽

2019 ◽

Vol 47 (16) ◽

pp. 8439-8451 ◽

Cited By ~ 1

Author(s):

Alberto González-Medina ◽

Elena Hidalgo ◽

José Ayté

Keyword(s):

Cell Cycle ◽

Molecular Mechanisms ◽

Histone H3 ◽

Dependent Manner ◽

Saga Complex ◽

Lysine Residues ◽

Physical Barriers ◽

A Cell ◽

Cycle Dependent ◽

Regulated Promoters

Abstract In fission yeast, MBF-dependent transcription is inactivated at the end of S phase through a negative feedback loop that involves the co-repressors, Yox1 and Nrm1. Although this repression system is well known, the molecular mechanisms involved in MBF activation remain largely unknown. Compacted chromatin constitutes a barrier to activators accessing promoters. Here, we show that chromatin regulation plays a key role in activating MBF-dependent transcription. Gcn5, a part of the SAGA complex, binds to MBF-regulated promoters through the MBF co-activator Rep2 in a cell cycle-dependent manner and in a reverse correlation to the binding of the MBF co-repressors, Nrm1 or Yox1. We propose that the co-repressors function as physical barriers to SAGA recruitment onto MBF promoters. We also show that Gcn5 acetylates specific lysine residues on histone H3 in a cell cycle-regulated manner. Furthermore, either in a gcn5 mutant or in a strain in which histone H3 is kept in an unacetylated form, MBF-dependent transcription is downregulated. In summary, Gcn5 is required for the full activation and correct timing of MBF-regulated gene transcription.

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Correction: Optineurin Regulates the Interferon Response in a Cell Cycle-Dependent Manner

PLoS Pathogens ◽

10.1371/journal.ppat.1004971 ◽

2015 ◽

Vol 11 (6) ◽

pp. e1004971 ◽

Cited By ~ 5

Author(s):

Pierre Génin ◽

Frédérique Cuvelier ◽

Sandrine Lambin ◽

Josina Côrte-Real Filipe ◽

Elodie Autrusseau ◽

...

Keyword(s):

Cell Cycle ◽

Interferon Response ◽

Dependent Manner ◽

A Cell ◽

Cycle Dependent

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Importin α/β-mediated nuclear protein import is regulated in a cell cycle-dependent manner

Experimental Cell Research ◽

10.1016/j.yexcr.2004.03.010 ◽

2004 ◽

Vol 297 (1) ◽

pp. 285-293 ◽

Cited By ~ 14

Author(s):

Noriko Yasuhara ◽

Eri Takeda ◽

Hitomi Inoue ◽

Ippei Kotera ◽

Yoshihiro Yoneda

Keyword(s):

Cell Cycle ◽

Protein Import ◽

Nuclear Protein ◽

Dependent Manner ◽

Importin Α ◽

A Cell ◽

Nuclear Protein Import ◽

Cycle Dependent

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Cks1 is degraded via the ubiquitin-proteasome pathway in a cell cycle-dependent manner

Genes to Cells ◽

10.1046/j.1365-2443.2003.00684.x ◽

2003 ◽

Vol 8 (11) ◽

pp. 889-896 ◽

Cited By ~ 13

Author(s):

Takayuki Hattori ◽

Kyoko Kitagawa ◽

Chiharu Uchida ◽

Toshiaki Oda ◽

Masatoshi Kitagawa

Keyword(s):

Cell Cycle ◽

Dependent Manner ◽

Ubiquitin Proteasome Pathway ◽

Ubiquitin Proteasome ◽

A Cell ◽

Proteasome Pathway ◽

Cycle Dependent

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Cyclin-dependent Kinases Phosphorylate p73 at Threonine 86 in a Cell Cycle-dependent Manner and Negatively Regulate p73

Journal of Biological Chemistry ◽

10.1074/jbc.m300251200 ◽

2003 ◽

Vol 278 (30) ◽

pp. 27421-27431 ◽

Cited By ~ 38

Author(s):

Christian Gaiddon ◽

Maria Lokshin ◽

Isabelle Gross ◽

Danielle Levasseur ◽

Yoichi Taya ◽

...

Keyword(s):

Cell Cycle ◽

Dependent Manner ◽

Cyclin Dependent Kinases ◽

A Cell ◽

Cycle Dependent

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The Gene Expression and Enzyme Activity of Plant 3-Deoxy-D-Manno-2-Octulosonic Acid-8-Phosphate Synthase Are Preferentially Associated with Cell Division in a Cell Cycle-Dependent Manner

PLANT PHYSIOLOGY ◽

10.1104/pp.103.026872 ◽

2003 ◽

Vol 133 (1) ◽

pp. 348-360 ◽

Cited By ~ 20

Author(s):

Frédéric Delmas ◽

Johann Petit ◽

Jérôme Joubès ◽

Martial Séveno ◽

Thomas Paccalet ◽

...

Keyword(s):

Gene Expression ◽

Cell Cycle ◽

Enzyme Activity ◽

Cell Division ◽

Dependent Manner ◽

A Cell ◽

Cycle Dependent ◽

Phosphate Synthase

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Regardless of the deposition pathway, aminoacid 31 in histone variant H3 is essential at gastrulation in Xenopus

10.1101/612515 ◽

2019 ◽

Author(s):

David Sitbon ◽

Ekaterina Boyarchuk ◽

Geneviève Almouzni

Keyword(s):

Cell Cycle ◽

Cell Fate ◽

Unique Property ◽

Dependent Manner ◽

Critical Importance ◽

Distinct Mode ◽

Developmental Defects ◽

A Cell ◽

Cycle Dependent ◽

Conserved Residue

AbstractThe closely related replicative H3 and non-replicative H3.3 variants show specific requirement during development in vertebrates. Whether it involves distinct mode of deposition or unique roles once incorporated into chromatin remains unclear. To disentangle the two aspects, we took advantage of the Xenopus early development combined with chromatin assays. Our previous work showed that in Xenopus, depletion of the non-replicative variant H3.3 impairs development at gastrulation, without compensation through provision of the replicative variant H3.2. We systematically mutated H3.3 at each four residues that differ from H3.2 and tested their ability to rescue developmental defects. Surprisingly, all H3.3 mutated variants functionally complemented endogenous H3.3, regardless of their incorporation pathways, except for one residue. This particular residue, the serine at position 31 in H3.3, gets phosphorylated onto chromatin in a cell cycle dependent manner. While the alanine substitution failed to rescue H3.3 depletion, a phosphomimic residue sufficed. We conclude that the time of gastrulation reveals a critical importance of the H3.3S31 residue independently of the variant incorporation pathway. We discuss how this single evolutionary conserved residue conveys a unique property for this variant in vertebrates during cell cycle and cell fate commitment.

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