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Related Experiment Videos

Effects of scaffold/matrix alteration on centromeric function and gene expression.

Huseyin Sumer1, Richard Saffery, Nicholas Wong

  • 1Murdoch Childrens Research Institute, Department of Pediatrics, Royal Children's Hospital, Flemington Road, Melbourne 3052, Australia.

The Journal of Biological Chemistry
|June 29, 2004
PubMed
Summary

Histone deacetylase inhibition and DNA intercalation drugs reduced scaffold/matrix attachment region (S/MAR) domain size at neocentromeres. This contraction did not impair centromere function or gene expression, suggesting S/MAR domain flexibility.

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Area of Science:

  • Epigenetics and Chromatin Biology
  • Molecular Genetics
  • Cell Biology

Background:

  • Human neocentromeres possess a 3.5-Mb scaffold/matrix attachment region (S/MAR) domain with normal gene expression.
  • Previous studies showed histone deacetylase inhibition (trichostatin A, TSA) shifted the CENP-A-binding domain without affecting mitotic segregation.

Purpose of the Study:

  • To investigate the effects of TSA and distamycin A (DST) on S/MAR domain size and neocentromere function.
  • To determine if S/MAR domain contraction impacts centromere integrity and gene transcription.

Main Methods:

  • Treatment of human neocentromeres with 33 nM TSA and 75 microg/ml DST.
  • Measurement of S/MAR and CENP-A-binding domain sizes.
  • Analysis of gene expression levels for 47 underlying genes.

Related Experiment Videos

  • Assessment of mitotic segregation and protein levels (Topo IIalpha, CENP-A, CENP-C, HP1alpha, BubR1).

    • Main Results:

    • TSA reduced the neocentromeric S/MAR domain to 1.7 Mb.
    • DST reduced the S/MAR domain to 1.2 Mb and the CENP-A-binding domain by 40% (to 196 kb) without positional shifts.
    • DST treatment led to chromosomal missegregation and altered protein levels.
    • Both TSA and DST reduced S/MAR domain size at a native chromosome 10 centromere.
    • No significant changes in the expression of 47 tested neocentromeric genes were observed with either treatment.

    Conclusions:

    • Substantial S/MAR domain contraction does not necessarily impair centromere function.
    • Disruption of the S/MAR domain affects binding of scaffold/matrix and centromeric proteins.
    • Neocentromeric chromatin exhibits transcriptional regulation similar to normal genomic sites.