Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2002-6-27
pubmed:abstractText
We have purified a human histone H4 lysine 20 methyltransferase and cloned the encoding gene, PR/SET07. A mutation in Drosophila pr-set7 is lethal: second instar larval death coincides with the loss of H4 lysine 20 methylation, indicating a fundamental role for PR-Set7 in development. Transcriptionally competent regions lack H4 lysine 20 methylation, but the modification coincided with condensed chromosomal regions on polytene chromosomes, including chromocenter and euchromatic arms. The Drosophila male X chromosome, which is hyperacetylated at H4 lysine 16, has significantly decreased levels of lysine 20 methylation compared to that of females. In vitro, methylation of lysine 20 and acetylation of lysine 16 on the H4 tail are competitive. Taken together, these results support the hypothesis that methylation of H4 lysine 20 maintains silent chromatin, in part, by precluding neighboring acetylation on the H4 tail.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1097-2765
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1201-13
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12086618-Acetylation, pubmed-meshheading:12086618-Amino Acid Sequence, pubmed-meshheading:12086618-Animals, pubmed-meshheading:12086618-Chromatin, pubmed-meshheading:12086618-Drosophila melanogaster, pubmed-meshheading:12086618-Female, pubmed-meshheading:12086618-HeLa Cells, pubmed-meshheading:12086618-Histone-Lysine N-Methyltransferase, pubmed-meshheading:12086618-Histones, pubmed-meshheading:12086618-Humans, pubmed-meshheading:12086618-Lysine, pubmed-meshheading:12086618-Male, pubmed-meshheading:12086618-Methylation, pubmed-meshheading:12086618-Methyltransferases, pubmed-meshheading:12086618-Microscopy, Fluorescence, pubmed-meshheading:12086618-Molecular Sequence Data, pubmed-meshheading:12086618-Nucleosomes, pubmed-meshheading:12086618-Protein Methyltransferases, pubmed-meshheading:12086618-Recombinant Fusion Proteins, pubmed-meshheading:12086618-Sequence Alignment
pubmed:year
2002
pubmed:articleTitle
PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin.
pubmed:affiliation
Howard Hughes Medical Institute, Division of Nucleic Acids Enzymology, Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't