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The Carboxyl-Terminal Region Common to Lamins A and C Contains a DNA Binding Domain

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Département de Biologie Supramoléculaire et Cellulaire, Institut Jacques Monod-CNRS UMR 7592, Universités Paris 6/Paris 7, 2 place Jussieu, 75251 Paris cedex 05, France, Département d'Ingénierie et d'Etudes des Protéines, Bat. 152, CEA Saclay, 91191 Gif-sur-Yvette, France, Departments of Medicine and of Anatomy and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, and Laboratoire de Minéralogie-Cristallographie Paris, CNRS UMR 7590, Universités Paris 6/Paris 7, 2 place Jussieu, 75251 Paris cedex 05, France
Cite this: Biochemistry 2003, 42, 17, 4819–4828
Publication Date (Web):April 9, 2003
Copyright © 2003 American Chemical Society

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    Lamins A and C are intermediate filament proteins which polymerize into the nucleus to form the nuclear lamina network. The lamina is apposed to the inner nuclear membrane and functions in tethering chromatin to the nuclear envelope and in maintaining nuclear shape. We have recently characterized a globular domain that adopts an immunoglobulin fold in the carboxyl-terminal tail common to lamins A and C. Using an electrophoretic mobility shift assay (EMSA), we show that a peptide containing this domain interacts in vitro with DNA after dimerization through a disulfide bond, but does not interact with the core particle or the dinucleosome. The covalent dimer binds a 30−40 bp DNA fragment with a micromolar affinity and no sequence specificity. Using nuclear magnetic resonance (NMR) and an EMSA, we observed that two peptide regions participate in the DNA binding:  the unstructured amino-terminal part containing the nuclear localization signal and a large positively charged region centered around amino acid R482 at the surface of the immunoglobulin-like domain. Mutations R482Q and -W, which are responsible for Dunnigan-type partial lipodystrophy, lower the affinity of the peptide for DNA. We conclude that the carboxyl-terminal end of lamins A and C binds DNA and suggest that alterations in lamin−DNA interactions may play a role in the pathophysiology of some lamin-linked diseases.

     This work was supported by the Centre National de la Recherche Scientifique, l'Institut National de la Santé et de la Recherche Médicale, and la Fondation pour la Recherche Médicale, by grants from FEGEFLUC and l'Association Française des Myopathies to S.Z.-J., and by grants from the American Diabetes Association and Human Frontiers Science Program to H.J.W.

     Institut Jacques Monod-CNRS UMR 7592, Universités Paris 6/Paris 7.


     CEA Saclay.

     Columbia University.

     CNRS UMR 7590, Universités Paris 6/Paris 7.


     To whom correspondence should be addressed. Phone:  33 1 44 27 77 63. Fax:  33 1 44 27 59 94. E-mail:  [email protected].

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    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

    Your Mendeley pairing has expired. Please reconnect