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Article

Structure and biochemical characterization of protein acetyltransferase from Sulfolobus solfataricus.

The Journal of biological chemistry - 17 Jul 2009

Brent Michael M, Iwata Ayaka, Carten Juliana, Zhao Kehao, Marmorstein Ronen

Abstract excerpt

The Sulfolobus solfataricus protein acetyltransferase (PAT) acetylates ALBA, an abundant nonspecific DNA-binding protein, on Lys(16) to reduce its DNA affinity, and the Sir2 deacetylase reverses the modification to cause transcriptional repression. This represents a "primitive" model for chromatin regulation analogous to histone modification in eukaryotes. We report the 1.84-A crystal structure of PAT in complex...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19473964
DOI: 10.1074/jbc.M109.014951
PMCID: PMC2740566

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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