The COOH-terminal domain of the JIL-1 histone H3S10 kinase interacts with histone H3 and is required for correct targeting to chromatin

Xiaomin Bao, Weili Cai, Huai Deng, Weiguo Zhang, Robert Krencik, Jack Girton, Jørgen Johansen, Kristen M Johansen

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

The JIL-1 histone H3S10 kinase in Drosophila localizes specifically to euchromatic interband regions of polytene chromosomes and is enriched 2-fold on the male X chromosome. JIL-1 can be divided into four main domains including an NH(2)-terminal domain, two separate kinase domains, and a COOH-terminal domain. Our results demonstrate that the COOH-terminal domain of JIL-1 is necessary and sufficient for correct chromosome targeting to autosomes but that both COOH- and NH(2)-terminal sequences are necessary for enrichment on the male X chromosome. We furthermore show that a small 53-amino acid region within the COOH-terminal domain can interact with the tail region of histone H3, suggesting that this interaction is necessary for the correct chromatin targeting of the JIL-1 kinase. Interestingly, our data indicate that the COOH-terminal domain alone is sufficient to rescue JIL-1 null mutant polytene chromosome defects including those of the male X chromosome. Nonetheless, we also found that a truncated JIL-1 protein which was without the COOH-terminal domain but retained histone H3S10 kinase activity was able to rescue autosome as well as partially rescue male X polytene chromosome morphology. Taken together these findings indicate that JIL-1 may participate in regulating chromatin structure by multiple and partially redundant mechanisms.

Original languageEnglish (US)
Pages (from-to)32741-50
Number of pages10
JournalThe Journal of biological chemistry
Volume283
Issue number47
DOIs
StatePublished - Nov 21 2008

Keywords

  • Animals
  • Chromatin
  • Chromosomes
  • Drosophila Proteins
  • Drosophila melanogaster
  • Gene Deletion
  • Histones
  • Microscopy, Fluorescence
  • Models, Biological
  • Molecular Conformation
  • Mutation
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein-Serine-Threonine Kinases
  • Recombinant Fusion Proteins
  • Journal Article
  • Research Support, N.I.H., Extramural

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