Association with the origin recognition complex suggests a novel role for histone acetyltransferase Hat1p/Hat2p View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2007-12

AUTHORS

Bernhard Suter, Oxana Pogoutse, Xinghua Guo, Nevan Krogan, Peter Lewis, Jack F Greenblatt, Jasper Rine, Andrew Emili

ABSTRACT

BACKGROUND: Histone modifications have been implicated in the regulation of transcription and, more recently, in DNA replication and repair. In yeast, a major conserved histone acetyltransferase, Hat1p, preferentially acetylates lysine residues 5 and 12 on histone H4. RESULTS: Here, we report that a nuclear sub-complex consisting of Hat1p and its partner Hat2p interacts physically and functionally with the origin recognition complex (ORC). While mutational inactivation of the histone acetyltransferase (HAT) gene HAT1 alone does not compromise origin firing or initiation of DNA replication, a deletion in HAT1 (or HAT2) exacerbates the growth defects of conditional orc-ts mutants. Thus, the ORC-associated Hat1p-dependent histone acetyltransferase activity suggests a novel linkage between histone modification and DNA replication. Additional genetic and biochemical evidence points to the existence of partly overlapping histone H3 acetyltransferase activities in addition to Hat1p/Hat2p for proper DNA replication efficiency. Furthermore, we demonstrated a dynamic association of Hat1p with chromatin during S-phase that suggests a role of this enzyme at the replication fork. CONCLUSION: We have found an intriguing new association of the Hat1p-dependent histone acetyltransferase in addition to its previously known role in nuclear chromatin assembly (Hat1p/Hat2p-Hif1p). The participation of a distinct Hat1p/Hat2p sub-complex suggests a linkage of histone H4 modification with ORC-dependent DNA replication. More... »

PAGES

38

Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1741-7007-5-38

DOI

http://dx.doi.org/10.1186/1741-7007-5-38

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1001133220

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17880717


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