Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state

FEBS Lett. 1996 Feb 12;380(1-2):161-4. doi: 10.1016/0014-5793(96)00034-8.

Abstract

The nuclear matrix maintains specific interactions with genomic DNA at sites known as matrix attachment regions (M/SARs). M/SARs bind in vitro to lamin polymers. We show that the polymerized alpha-helical rod domain of lamin Dm0 provides by itself the specific binding to the ftz M/SAR. In contrast, unpolymerized rod domain does not bind specifically to this M/SAR. Non-specific binding to DNA is also observed with Dm0 containing a point mutation that impairs its ability to polymerize or with the isolated tail domain. These data suggest that the specific binding of lamins to M/SARs requires the rod domain and depends on the lamin polymerization state.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallization
  • DNA / metabolism*
  • Drosophila Proteins*
  • Drosophila melanogaster
  • Fushi Tarazu Transcription Factors
  • Homeodomain Proteins / genetics
  • Lamins
  • Molecular Sequence Data
  • Nuclear Matrix / metabolism*
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Point Mutation
  • Polymers / metabolism
  • Protein Binding
  • Protein Conformation

Substances

  • Drosophila Proteins
  • Fushi Tarazu Transcription Factors
  • Homeodomain Proteins
  • Lam protein, Drosophila
  • Lamins
  • Nuclear Proteins
  • Polymers
  • ftz protein, Drosophila
  • DNA