Výsledky vyhledávání - "L. G. Chicoine"

Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena. Evidence for functionally distinct H4 acetylation sites

Autor: R Richman, C D Allis, Richard G. Cook, Ira G. Schulman, L G Chicoine

Publikováno v: Journal of Biological Chemistry. 261:1071-1076

Macro- and micronuclei of the ciliated protozoan Tetrahymena thermophila afford a unique opportunity to study histone acetylation under conditions where postsynthetic "transcription"-related acetylation and synthetic "deposition"-related acetylation

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::c8349b8648cb8d3ed73098b0ff818965
https://doi.org/10.1016/s0021-9258(17)36054-4

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Modulation of linker histones during development in Tetrahymena: Selective elimination of linker histone during the differentiation of new macronuclei

Autor: C D Allis, Wiggins Jc, R Richman, Wenkert D, L G Chicoine

Publikováno v: Developmental Biology. 109:1-8

Macronuclei of Tetrahymena thermophila contain a typical H1 which has been shown to be missing from micronuclei. Instead, micronuclei contain three unique polypeptides, alpha, beta, and gamma, which are associated with linker regions of micronuclear

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51177798a3623b8fa644110bca9c54dc
https://doi.org/10.1016/0012-1606(85)90339-2

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A single histone acetyltransferase from Tetrahymena macronuclei catalyzes deposition-related acetylation of free histones and transcription-related acetylation of nucleosomal histones

Autor: R Richman, L G Chicoine, C D Allis, Martin A. Gorovsky, Richard G. Cook

Publikováno v: The Journal of Cell Biology

A salt-extracted histone acetyltransferase activity from Tetrahymena macronuclei acetylates mostly histone H3 and H4 when free histones are used as substrate. Free histone H4 is acetylated first at position 11 (monoacetylated) or positions 11 and 4 (

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::999a9782e48d3edb988bce24963417a4
http://europepmc.org/articles/PMC2114890

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Autor: R Richman, C D Allis, L G Chicoine, Ira G. Schulman

Publikováno v: Proceedings of the National Academy of Sciences. 82:8048-8052

Macro- and micronuclei of the ciliated protozoan, Tetrahymena thermophila, afford a unique opportunity to study histone acetylation under conditions where acetylation associated with the regulation of transcription and acetylation associated with the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4dda5109123df299ce34d10853162b2
https://doi.org/10.1073/pnas.82.23.8048

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Proteolytic processing of h1-like histones in chromatin: a physiologically and developmentally regulated event in Tetrahymena micronuclei

Autor: L G Chicoine, R Richman, J C Wiggins, C D Allis, R L Allen

Publikováno v: The Journal of Cell Biology

Micronuclei isolated from growing cells of Tetrahymena thermophila contain three H1-like polypeptides alpha, beta, and gamma. Micronuclei isolated from young conjugating cells (3-7 h) also contain a larger molecular weight polypeptide, X, which is be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60c56138239171fa4aad307124b32025
http://europepmc.org/articles/PMC2113348

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Nonrandom utilization of acetylation sites in histones isolated from Tetrahymena. Evidence for functionally distinct H4 acetylation sites

Autor: L G, Chicoine, I G, Schulman, R, Richman, R G, Cook, C D, Allis

Publikováno v: The Journal of biological chemistry. 261(3)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e80b0bc5f43bc5bec01e0da019a48a4c
https://pubmed.ncbi.nlm.nih.gov/3080415

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Regulation of histone acetylation during macronuclear differentiation in Tetrahymena: evidence for control at the level of acetylation and deacetylation

Autor: C D Allis, L G Chicoine

Publikováno v: Developmental biology. 116(2)

During the postzygotic period of the sexual cycle (conjugation) in the ciliated protozoan, Tetrahymena, daughter products from a single micronuclear mitotic division develop into new macronuclei (anlagen) or new micronuclei depending upon their cytop

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::750507564e5f0424689a5985599e3d20
https://pubmed.ncbi.nlm.nih.gov/3732617

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Micronuclei and the cytoplasm of growing Tetrahymena contain a histone acetylase activity which is highly specific for free histone H4

Autor: Richard G. Cook, M P Collini, L G Chicoine, R Richman, C D Allis

Publikováno v: The Journal of Cell Biology

Salt extracts prepared from purified micronuclei and the cytoplasm of growing Tetrahymena contain a histone acetylase (also referred to as histone acetyltransferase) activity which is highly specific for H4 when tested as a free histone. With both ex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f20e7b3b0c0fb5d2a016c3cfc7c0ee68
https://pubmed.ncbi.nlm.nih.gov/3360847

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