Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci.
We have shown previously that a stretch of four charged residues (16-19) at the histone H4 N-terminus is involved in repression of the yeast silent mating loci. One of these residues, Lys16, is a site for acetylation, which may prevent repression of the silent mating loci. In this paper we ask whether other sequences in histone H4, possibly in conjunction with H3 residues, are required for repression. We find that even in combination, the other seven acetylatable lysines in H3 and H4 do not function in repression. In contrast, we have found that an adjacent relatively uncharged domain (residues 21-29) is required for repression and that single amino acid insertions and deletions in this region are extremely detrimental. We propose that the basic and non-basic domains together form a DNA (or protein) induced amphipathic alpha-helix required in the formation of a repressive chromatin structure.
Johnson
L M
LM
Molecular Biology Institute, University of California, Los Angeles 90024.
Fisher-Adams
G
G
Grunstein
M
M
D000107:Acetylation; D000595:Amino Acid Sequence; D003433:Crosses, Genetic; D015966:Gene Expression Regulation, Fungal; D005800:Genes, Fungal; D006657:Histones / Q000235:genetics* / Q000378:metabolism*; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D010957:Plasmids; D016133:Polymerase Chain Reaction / Q000379:methods; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000502:physiology
D006657:Histones