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Cited by 349

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Genetic Analysis of Histone H4: Essential Role of Lysines Subject to Reversible Acetylation

Megee, Paul C., Morgan, Brian A., Mittman, Barbara A., Smith, M. Mitchell·1990·Science

Abstract

The nucleosome is the fundamental unit of assembly of the chromosome and reversible modifications of the histones have been suggested to be important in many aspects of nucleosome function. The structure-function relations of the amino-terminal domain of yeast histone H4 were examined by the creation of directed point mutations. The four lysines subject to reversible acetylation were essential for histone function as the substitution of arginine or asparagine at these four positions was lethal. No single lysine residue was completely essential since arginine substitutions at each position were viable, although several of these mutants were slower in completing DNA replication. The simultaneous substitution of glutamine for the four lysine residues was viable but conferred several phenotypes including mating sterility, slow progression through the G 2 /M period of the division cycle, and temperature-sensitive growth, as well as a prolonged period of DNA replication. These results provide genetic proof for the roles of the H4 amino-terminal domain lysines in gene expression, replication, and nuclear division.

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Metadata

Authors
Megee, P. C., Morgan, B. A., Mittman, B. A., & Smith, M. M.
Venue
Science
Published
1990-02-16
Volume
247
Issue
4944
Pages
841-845
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1966792552
Cited by
349
References
32
FWCI
8.64
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Genetic Analysis of Histone H4: Essential Role of Lysines Subject to Reversible Acetylation. https://app.cochat.ai/papers/10.1126/science.2106160
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Megee, P. C., Morgan, B. A., Mittman, B. A., & Smith, M. M. (1990). Genetic Analysis of Histone H4: Essential Role of Lysines Subject to Reversible Acetylation. Science. https://doi.org/10.1126/science.2106160

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