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Liokatis, S.* ; Edlich, C.* ; Soupsana, K.* ; Giannios, I.* ; Panagiotidou, P.* ; Tripsianes, K. ; Sattler, M. ; Georgatos, S.D.* ; Politou, A.S.*

Solution structure and molecular interactions of lamin B receptor Tudor domain.

J. Biol. Chem. 287, 1032-1042 (2012)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
Lamin B receptor (LBR) is a polytopic protein of the nuclear envelope thought to connect the inner nuclear membrane with the underlying nuclear lamina and peripheral heterochromatin. To better understand the function of this protein, we have examined in detail its nucleoplasmic region, which is predicted to harbor a Tudor domain (LBR-TD). Structural analysis by multidimensional NMR spectroscopy establishes that LBR-TD indeed adopts a classical β-barrel Tudor fold in solution, which, however, features an incomplete aromatic cage. Removal of LBR-TD renders LBR more mobile at the plane of the nuclear envelope, but the isolated module does not bind to nuclear lamins, heterochromatin proteins (MeCP2), and nucleosomes, nor does it associate with methylated Arg/Lys residues through its aromatic cage. Instead, LBR-TD exhibits tight and stoichiometric binding to the "histone-fold" region of unassembled, free histone H3, suggesting an interesting role in histone assembly. Consistent with such a role, robust binding to native nucleosomes is observed when LBR-TD is extended toward its carboxyl terminus, to include an area rich in Ser-Arg residues. The Ser-Arg region, alone or in combination with LBR-TD, binds both unassembled and assembled H3/H4 histones, suggesting that the TD/RS interface may operate as a "histone chaperone-like platform."
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords INNER NUCLEAR-MEMBRANE; HISTONE H3; PROTEIN LBR; ARGININE RESIDUES; NMR EXPERIMENTS; DNA-REPAIR; BINDING; RECOGNITION; ENVELOPE; SMN
ISSN (print) / ISBN 0021-9258
e-ISSN 1083-351X
Journal Journal of Biological Chemistry, The
Quellenangaben Volume: 287, Issue: 2, Pages: 1032-1042 Article Number: , Supplement: ,
Publisher American Society for Biochemistry and Molecular Biology
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)