Regulation of gene transcription by the histone H2A N-terminal domain.
Histone N-terminal domains play critical roles in regulating chromatin structure and gene transcription. Relatively little is known, however, about the role of the histone H2A N-terminal domain in transcription regulation. We have used DNA microarrays to characterize the changes in genome-wide expression caused by mutations in the N-terminal domain of histone H2A. Our results indicate that the N-terminal domain of histone H2A functions primarily to repress the transcription of a large subset of the Saccharomyces cerevisiae genome and that most of the H2A-repressed genes are also repressed by the histone H2B N-terminal domain. Using the histone H2A microarray data, we selected three reporter genes (BNA1, BNA2, and GCY1), which we subsequently used to map regions in the H2A N-terminal domain responsible for this transcriptional repression. These studies revealed that a small subdomain in the H2A N-terminal tail, comprised of residues 16 to 20, is required for the transcriptional repression of these reporter genes. Deletion of either the entire histone H2A N-terminal domain or just this small subdomain imparts sensitivity to UV irradiation. Finally, we show that two residues in this H2A subdomain, serine-17 and arginine-18, are specifically required for the transcriptional repression of the BNA2 reporter gene.
Parra
Michael A
MA
School of Molecular Biosciences, Washington State University, Fulmer Hall 675, Pullman, WA 99164-4660, USA.
Wyrick
John J
JJ
D050561:3-Hydroxyanthranilate 3,4-Dioxygenase / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D015966:Gene Expression Regulation, Fungal / Q000528:radiation effects; D005800:Genes, Fungal; D006657:Histones / Q000737:chemistry* / Q000378:metabolism*; D008239:Lysine / Q000378:metabolism; D008969:Molecular Sequence Data; D016296:Mutagenesis; D009154:Mutation / Q000235:genetics; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000235:genetics* / Q000528:radiation effects; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D020539:Sequence Analysis, Protein; D017384:Sequence Deletion; D013329:Structure-Activity Relationship; D014158:Transcription, Genetic / Q000528:radiation effects; D014466:Ultraviolet Rays
D006657:Histones; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D050561:3-Hydroxyanthranilate 3,4-Dioxygenase; C493361:BNA1 protein, S cerevisiae; D008239:Lysine