A Database of Drosophila Genes & Genomes

FB2013_03, released May 7th, 2013
 

Reference Report

Reference
Citation Zhao, K., Harel, A., Stuurman, N., Guedalia, D., Gruenbaum, Y. (1996). Binding of matrix attachment regions to nuclear lamin is mediated by the rod domain and depends on the lamin polymerization state.  FEBS Lett. 380(1-2): 161--164. (Export to RIS)
FlyBase ID FBrf0087806
Publication Type Research paper
PubMed ID 8603728
PubMed 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.
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Language of Publication English
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Publication Type Journal
Abbreviation FEBS Lett.
Title FEBS Letters
Publication Year 1968-
ISBN/ISSN 0014-5793
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