Journal ArticleDOI
Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation.
Michael J. Hendzel,Y Wei,Michael A. Mancini,A. Van Hooser,Tamara A. Ranalli,Bill R. Brinkley,David P. Bazett-Jones,C D Allis +7 more
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TLDR
It is proposed that the singular phosphorylation of the amino-terminus of histone H3 may be involved in facilitating two key functions during mitosis: (1) regulate protein-protein interactions to promote binding of trans-acting factors that “drive” chromatin condensation as cells enter M-phase and (2) coordinate chromatin decondensation associated with M- phase.Abstract:
We have generated and characterized a novel site-specific antibody highly specific for the phosphorylated form of the amino-terminus of histone H3 (Ser10). In this study, we used this antibody to examine in detail the relationship between H3 phosphorylation and mitotic chromosome condensation in mammalian cells. Our results extend previous biochemical studies by demonstrating that mitotic phosphorylation of H3 initiates nonrandomly in pericentromeric heterochromatin in late G2 interphase cells. Following initiation, H3 phosphorylation appears to spread throughout the condensing chromatin and is complete in most cell lines just prior to the formation of prophase chromosomes, in which a phosphorylated, but nonmitotic, chromosomal organization is observed. In general, there is a precise spatial and temporal correlation between H3 phosphorylation and initial stages of chromatin condensation. Dephosphorylation of H3 begins in anaphase and is complete immediately prior to detectable chromosome decondensation in telophase cells. We propose that the singular phosphorylation of the amino-terminus of histone H3 may be involved in facilitating two key functions during mitosis: (1) regulate protein-protein interactions to promote binding of trans-acting factors that "drive" chromatin condensation as cells enter M-phase and (2) coordinate chromatin decondensation associated with M-phase.read more
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Journal ArticleDOI
The language of covalent histone modifications.
Brian D. Strahl,C D Allis +1 more
TL;DR: It is proposed that distinct histone modifications, on one or more tails, act sequentially or in combination to form a ‘histone code’ that is, read by other proteins to bring about distinct downstream events.
Journal ArticleDOI
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Stephen Rea,Frank Eisenhaber,Dónal O'Carroll,Brian D. Strahl,Zu-Wen Sun,Manfred Schmid,Susanne Opravil,Karl Mechtler,Chris P. Ponting,C D Allis,Thomas Jenuwein +10 more
TL;DR: A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
Journal ArticleDOI
A Lentiviral RNAi Library for Human and Mouse Genes Applied to an Arrayed Viral High-Content Screen
Jason Moffat,Dorre A. Grueneberg,Xiaoping Yang,So Young Kim,So Young Kim,Angela M. Kloepfer,Gregory Hinkle,Gregory Hinkle,Bruno Piqani,Thomas Eisenhaure,Biao Luo,Jennifer K. Grenier,Anne E. Carpenter,Shi Yin Foo,Sheila A. Stewart,Brent R. Stockwell,Nir Hacohen,Nir Hacohen,William C. Hahn,William C. Hahn,Eric S. Lander,David M. Sabatini,David M. Sabatini,David E. Root +23 more
TL;DR: A screen based on high-content imaging was developed to identify genes required for mitotic progression in human cancer cells and applied to an arrayed set of 5,000 unique shRNA-expressing lentiviruses that target 1,028 human genes, providing a widely applicable resource for loss-of-function screens.
Journal ArticleDOI
Loss of the Suv39h histone methyltransferases impairs mammalian heterochromatin and genome stability.
Antoine H.F.M. Peters,Dónal O'Carroll,Harry Scherthan,Karl Mechtler,Stephan Sauer,Christian Schöfer,Klara Weipoltshammer,Michaela Pagani,Monika Lachner,Alexander Kohlmaier,Susanne Opravil,Michael P. Doyle,Maria Sibilia,Thomas Jenuwein +13 more
TL;DR: In vivo data assign a crucial role for pericentric H3-K9 methylation in protecting genome stability, and define the Suv39h HMTases as important epigenetic regulators for mammalian development.
Journal ArticleDOI
Histone acetylation and an epigenetic code
TL;DR: Recent evidence raises the interesting possibility that an acetylation-based code may operate through both mitosis and meiosis, providing a possible mechanism for germ-line transmission of epigenetic changes.
References
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Journal ArticleDOI
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
Journal Article
Cleavage of structural proteins during the assemble of the head of bacterio-phage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products as mentioned in this paper.
Journal ArticleDOI
Delineation of individual human chromosomes in metaphase and interphase cells by in situ suppression hybridization using recombinant DNA libraries
TL;DR: A method of in situ hybridization for visualizing individual human chromosomes from pter to qter, both in metaphase spreads and interphase nuclei, is reported and should be useful for both karyotypic studies and for the analysis of chromosome topography in interphase cells.
Journal ArticleDOI
Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
TL;DR: It is shown that the SIR3 and SIR4 proteins interact with specific silencing domains of the H3 and H4 N-termini in vitro, which proposes a model for heterochromatin-mediated transcriptional silencing in yeast, which may serve as a paradigm for other eukaryotic organisms as well.
Journal ArticleDOI
Topoisomerase II is a structural component of mitotic chromosome scaffolds
TL;DR: The results suggest that topoisomerase II may be an enzyme that is also a structural protein of interphase nuclei and mitotic chromosomes, and an abundant nuclear enzyme that controls DNA topological states.