Mitotic phosphorylation of histone H3 at threonine 3.
FEBS Lett
; 560(1-3): 39-44, 2004 Feb 27.
Article
em En
| MEDLINE
| ID: mdl-14987995
ABSTRACT
Nuclear envelope-peripheral heterochromatin fractions contain multiple histone kinase activities. In vitro assays and amino-terminal sequencing show that one of these activities co-isolates with heterochromatin protein 1 (HP1) and phosphorylates histone H3 at threonine 3. Antibodies recognizing this post-translational modification reveal that in vivo phosphorylation at threonine 3 commences at early prophase in the vicinity of the nuclear envelope, spreads to pericentromeric chromatin during prometaphase and is fully reversed by late anaphase. This spatio-temporal pattern is distinct from H3 phosphorylation at serine 10, which also occurs during cell division, suggesting segregation of differentially phosphorylated chromatin to different regions of mitotic chromosomes.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Treonina
/
Histonas
Limite:
Animals
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2004
Tipo de documento:
Article
País de afiliação:
Grécia