Expression profiling of S. pombe acetyltransferase mutants identifies redundant pathways of gene regulation

BMC Genomics

Research Article

Anthony PH Wright¹  Anna Johnsson¹  Yongtao Xue-Franzén¹  Rebecca L Nugent²  Susan L Forsburg²  Chris Seidel³  Madelaine Gogol³  Brian Fleharty³ 

[1] Center for Biosciences, Department of Biosciences and Nutrition, Karolinska Institutet, S-141-57 Huddinge, Sweden and School of Life Sciences, Södertörn University, S-141 89, Huddinge, Sweden;Molecular and Computational Biology Section, University of Southern California, 90089-2910, Los Angeles, California, USA;Stowers Institute for Medical Research, 64110, Kansas CityMissouri, USA;

关键词: Gene Ontology;    Double Mutant;    Fission Yeast;    Triple Mutant;    H3K14 Acetylation;   

DOI  :  10.1186/1471-2164-11-59

 received in 2009-08-13, accepted in 2010-01-22,  发布年份 2010

来源: Springer

【 摘 要 】

BackgroundHistone acetyltransferase enzymes (HATs) are implicated in regulation of transcription. HATs from different families may overlap in target and substrate specificity.ResultsWe isolated the elp3+ gene encoding the histone acetyltransferase subunit of the Elongator complex in fission yeast and characterized the phenotype of an Δelp3 mutant. We examined genetic interactions between Δelp3 and two other HAT mutants, Δmst2 and Δgcn5 and used whole genome microarray analysis to analyze their effects on gene expression.ConclusionsComparison of phenotypes and expression profiles in single, double and triple mutants indicate that these HAT enzymes have overlapping functions. Consistent with this, overlapping specificity in histone H3 acetylation is observed. However, there is no evidence for overlap with another HAT enzyme, encoded by the essential mst1+ gene.

【 授权许可】

Unknown   
© Nugent et al; licensee BioMed Central Ltd. 2010. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.