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

FEBS Letters
K ZhaoY Gruenbaum

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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Citations

Sep 10, 2010·Cold Spring Harbor Perspectives in Biology·Thomas DechatRobert D Goldman
Mar 17, 1999·Proceedings of the National Academy of Sciences of the United States of America·M GoldbergY Gruenbaum
Jan 16, 2008·The Journal of Cell Biology·R Ileng Kumaran, David L Spector
Jan 22, 2009·Advances in Enzyme Regulation·Thomas DechatRobert D Goldman
Feb 13, 2009·Journal of Cellular and Molecular Medicine·Miron ProkocimerYosef Gruenbaum
Feb 10, 2011·Wiley Interdisciplinary Reviews. Systems Biology and Medicine·David W Van de VosseJohn D Aitchison
Nov 20, 2015·Open Biology·Magdalena MachowskaRyszard Rzepecki
Jun 18, 2002·Journal of Structural Biology·Yonatan B TzurYosef Gruenbaum
Sep 2, 1998·Journal of Structural Biology·N StuurmanU Aebi
Sep 8, 2016·Frontiers in Genetics·Jérôme D Robin, Frédérique Magdinier
Jul 3, 2017·Journal of Cell Science·Nana NaetarRoland Foisner
Nov 5, 1999·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·N Chaly, U Stochaj
Jun 25, 1998·Molecular and Cellular Biology·M GoldbergM F Wolfner
Apr 16, 2020·Aging Cell·Filipa MartinsSandra Rebelo
Jan 8, 2021·Frontiers in Cell and Developmental Biology·Tanaya Roychowdhury, Samit Chattopadhyay
Mar 6, 2002·Genes & Development·Robert D GoldmanTimothy P Spann

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