title: Purification and Structural Analysis of LEM-Domain Proteins.
abstract: LAP2-emerin-MAN1 (LEM)-domain proteins are modular proteins characterized by the presence of a conserved motif of about 50 residues. Most LEM-domain proteins localize at the inner nuclear membrane, but some are also found in the endoplasmic reticulum or nuclear interior. Their architecture has been analyzed by predicting the limits of their globular domains, determining the 3D structure of these domains and in a few cases calculating the 3D structure of specific domains bound to biological targets. The LEM domain adopts an α-helical fold also found in SAP and HeH domains of prokaryotes and unicellular eukaryotes. The LEM domain binds to BAF (barrier-to-autointegration factor; BANF1), which interacts with DNA and tethers chromatin to the nuclear envelope. LAP2 isoforms also share an N-terminal LEM-like domain, which binds DNA. The structure and function of other globular domains that distinguish LEM-domain proteins from each other have been characterized, including the C-terminal dimerization domain of LAP2α and C-terminal WH and UHM domains of MAN1. LEM-domain proteins also have large intrinsically disordered regions that are involved in intra- and intermolecular interactions and are highly regulated by posttranslational modifications in vivo.
authors.affiliation: Institute for Integrative Biology of the Cell, CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, Paris, France.
authors.forename: Isaline
authors.initials: I
authors.lastname: Herrada
authors.affiliation: Institute for Integrative Biology of the Cell, CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, Paris, France.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Bourgeois
authors.affiliation: Institute for Integrative Biology of the Cell, CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, Paris, France.
authors.forename: Camille
authors.initials: C
authors.lastname: Samson
authors.affiliation: Institut de Biologie Fonctionnelle et Adaptative, Université Paris Diderot, Paris, France.
authors.forename: Brigitte
authors.initials: B
authors.lastname: Buendia
authors.affiliation: Department of Medicine, College of Physicians and Surgeons, Columbia University, New York, USA; Department of Pathology and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, USA.
authors.forename: Howard J
authors.initials: HJ
authors.lastname: Worman
authors.affiliation: Institute for Integrative Biology of the Cell, CEA, CNRS, Université Paris-Sud, Gif-sur-Yvette, Paris, France. Electronic address: sophie.zinn@cea.fr.
authors.forename: Sophie
authors.initials: S
authors.lastname: Zinn-Justin
mesh_terms: D002853:Chromatography, Liquid; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000302:isolation & purification*; D004926:Escherichia coli; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000302:isolation & purification*; D019906:Nuclear Magnetic Resonance, Biomolecular; D009687:Nuclear Proteins / Q000737:chemistry / Q000302:isolation & purification*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D017433:Protein Structure, Secondary
chemical_list: D004268:DNA-Binding Proteins; C405329:LEMD3 protein, human; D008565:Membrane Proteins; D009687:Nuclear Proteins; C092710:emerin; C093413:lamina-associated polypeptide 2
keywords: Assembly; Chromatin; Disease; Envelopathy; Inner nuclear membrane; Interaction; Lamin; Nuclear magnetic resonance; Purification; Structure