Histone H2A.Z Acetylation Modulates an Essential Charge Patch

Histone H2A.Z is structurally and functionally distinct from the major H2As. To understand the function of H2A.Z acetylation, we performed a mutagenic analysis of the six acetylated lysines in the N-terminal tail of Tetrahymena H2A.Z. Tetrahymena cannot survive with arginines at all six sites. Reten...

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Bibliographic Details
Published in:Molecular cell 2001-06, Vol.7 (6), p.1329-1335
Main Authors: Ren, Qinghu, Gorovsky, Martin A.
Format: Article
Language:English
Subjects:
Acetylation
Animals
Arginine - genetics
Arginine - metabolism
Electrochemistry
Gene Deletion
Glutamine - genetics
Glutamine - metabolism
histone H2A.Z
Histones - genetics
Histones - metabolism
Lysine - genetics
Lysine - metabolism
Mutagenesis, Site-Directed
Tetrahymena
Tetrahymena thermophila - genetics
Tetrahymena thermophila - growth & development
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Summary:Histone H2A.Z is structurally and functionally distinct from the major H2As. To understand the function of H2A.Z acetylation, we performed a mutagenic analysis of the six acetylated lysines in the N-terminal tail of Tetrahymena H2A.Z. Tetrahymena cannot survive with arginines at all six sites. Retention of one acetylatable lysine is sufficient to provide the essential function of H2A.Z acetylation. This essential function can be mimicked by deleting the region encompassing all six sites, or by mutations that reduce the positive charge of the N terminus at the acetylation sites themselves, or at other sites in the tail. These properties argue that the essential function of H2A.Z acetylation is to modify a “charge patch” by reducing the charge of the tail.
ISSN:1097-2765
1097-4164
DOI:10.1016/S1097-2765(01)00269-6