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C. D. Allis

Researcher at Syracuse University

Publications -  7
Citations -  1077

C. D. Allis is an academic researcher from Syracuse University. The author has contributed to research in topics: Acetylation & Tetrahymena. The author has an hindex of 7, co-authored 7 publications receiving 1058 citations.

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Journal ArticleDOI

Transcriptional silencing in yeast is associated with reduced nucleosome acetylation

TL;DR: The hypothesis that silencing in yeast results from heterochromatin formation is fortified and it is argued that the silencing proteins participate in this formation.
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Non-random acetylation of histone H4 by a cytoplasmic histone acetyltransferase as determined by novel methodology.

TL;DR: These data show remarkable preference for lysine 11/12 by the Drosophila HAT B activity in vitro and provide support for the assertion that this activity functions to acetylate new H4, at least in part, for deposition and chromatin assembly in vivo.
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Proteolytic removal of core histone amino termini and dephosphorylation of histone H1 correlate with the formation of condensed chromatin and transcriptional silencing during Tetrahymena macronuclear development.

TL;DR: The results strongly suggest that the developmentally regulated proteolysis of core histones and dephosphorylation of histone H1 participate in a novel pathway leading to the formation of highly condensed chromatin and transcriptional silencing during Tetrahymena macronuclear development.
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Macronuclei and micronuclei in Tetrahymena thermophila contain high-mobility-group-like chromosomal proteins containing a highly conserved eleven-amino-acid putative DNA-binding sequence.

TL;DR: Surprisingly, a linker histone found exclusively in transcriptionally inactive micronuclei also has several HMG-like characteristics, including the ability to be specifically extracted from nuclei by elutive intercalation and the presence of the HMG 1 box, which suggests that at least in T. thermophila, proteins with H MG-like properties are not restricted to regions of transcriptionally active chromatin.
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An abundant high-mobility-group-like protein is targeted to micronuclei in a cell cycle-dependent and developmentally regulated fashion in Tetrahymena thermophila.

TL;DR: It is demonstrated for the first time that an abundant high-mobility-group (HMG)-like protein, HMG B, previously thought to be specific to macron nuclei in Tetrahymena thermophila, is also present in micronuclei, and supports a model wherein H MG B functions to wrap DNA, presumably modulating higher-order chromatin structure for a broad range of biological processes, including transcription and replication.