Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state.
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.
Zhao
K
K
Department of Genetics, Life Sciences Institute, Hebrew University of Jerusalem, Israel.
Harel
A
A
Stuurman
N
N
Guedalia
D
D
Gruenbaum
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D003460:Crystallization; D004247:DNA / Q000378:metabolism*; D029721:Drosophila Proteins; D004331:Drosophila melanogaster; D051717:Fushi Tarazu Transcription Factors; D018398:Homeodomain Proteins / Q000235:genetics; D034882:Lamins; D008969:Molecular Sequence Data; D015530:Nuclear Matrix / Q000378:metabolism*; D009687:Nuclear Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017354:Point Mutation; D011108:Polymers / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation
D029721:Drosophila Proteins; D051717:Fushi Tarazu Transcription Factors; D018398:Homeodomain Proteins; C440328:Lam protein, Drosophila; D034882:Lamins; D009687:Nuclear Proteins; D011108:Polymers; C497169:ftz protein, Drosophila; D004247:DNA