Analysis of the role of Aurora B on the chromosomal targeting of condensin I

During mitosis, chromosome condensation takes place, which entails the conversion of interphase chromatin into compacted mitotic chromosomes. Condensin I is a five-subunit protein complex that plays a central role in this process. Condensin I is targeted to chromosomes in a mitosis-specific manner,...

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Bibliographic Details
Published in:Nucleic acids research 2007-04, Vol.35 (7), p.2403-2412
Main Authors: Takemoto, Ai, Murayama, Akiko, Katano, Miyuki, Urano, Takeshi, Furukawa, Koichi, Yokoyama, Shigeyuki, Yanagisawa, Junn, Hanaoka, Fumio, Kimura, Keiji
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Animals
Aurora Kinase B
Chromosomes - metabolism
DNA-Binding Proteins - metabolism
Interphase
Mitosis
Molecular Biology
Multiprotein Complexes - metabolism
Okadaic Acid - pharmacology
Ovum - enzymology
Protein-Serine-Threonine Kinases - antagonists & inhibitors
Protein-Serine-Threonine Kinases - physiology
Xenopus
Xenopus Proteins - antagonists & inhibitors
Xenopus Proteins - physiology
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Summary:During mitosis, chromosome condensation takes place, which entails the conversion of interphase chromatin into compacted mitotic chromosomes. Condensin I is a five-subunit protein complex that plays a central role in this process. Condensin I is targeted to chromosomes in a mitosis-specific manner, which is regulated by phosphorylation by mitotic kinases. Phosphorylation of histone H3 at serine 10 (Ser10) occurs during mitosis and its physiological role is a longstanding question. We examined the function of Aurora B, a kinase that phosphorylates Ser10, in the chromosomal binding of condensin I and mitotic chromosome condensation, using an in vitro system derived from Xenopus egg extract. Aurora B depletion from a mitotic egg extract resulted in the loss of H3 phosphorylation, accompanied with a 50% reduction of chromosomal targeting of condensin I. Alternatively, a portion of condensin I was bound to sperm chromatin, and chromosome-like structures were assembled when okadaic acid (OA) was supplemented in an interphase extract that lacks Cdc2 activity. However, chromosomal targeting of condensin I was abolished when Aurora B was depleted from the OA-treated interphase extract. From these results, it is suggested that Aurora B-dependent and Cdc2-independent pathways of the chromosomal targeting of condensin I are present.
ISSN:0305-1048
1362-4962
DOI:10.1093/nar/gkm157