Histones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1 (Journal article)

Polioudaki, H./ Kourmouli, N./ Drosou, V./ Bakou, A./ Theodoropoulos, P. A./ Singh, P. B./ Giannakouros, T./ Georgatos, S. D.


We have recently shown that heterochromatin protein 1 (HP1) interacts with the nuclear envelope in an acetylation-dependent manner. Using purified components and in vitro assays, we now demonstrate that HP1 forms a quaternary complex with the inner nuclear membrane protein LBR and a sub-set of core histones. This complex involves histone H3/H4 oligomers, which mediate binding of LBR to HP1 and cross-link these two proteins that do not interact directly with each other. Consistent with previous observations, HP1 and LBR binding to core histones is strongly inhibited when H3/H4 are modified by recombinant CREB-binding protein, revealing a new mechanism for anchoring domains of under-acetylated chromatin to the inner nuclear membrane.
Institution and School/Department of submitter: Πανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικής
Keywords: Acetylation,Animals,Binding Sites,Blotting, Western,Cell Nucleus/metabolism,Dose-Response Relationship, Drug,Electrophoresis, Polyacrylamide Gel,Fishes,Glutathione Transferase/metabolism,Heterochromatin/metabolism,Histones/*metabolism,Intracellular Membranes/metabolism,Mice,Models, Biological,Plasmids/metabolism,Precipitin Tests,Protein Binding,Protein Structure, Tertiary,Recombinant Fusion Proteins/metabolism,Recombinant Proteins/metabolism,Turkeys
URI: http://olympias.lib.uoi.gr/jspui/handle/123456789/21194
ISSN: 1469-221X
Link: http://www.ncbi.nlm.nih.gov/pubmed/11571267
http://www.nature.com/embor/journal/v2/n10/pdf/embor322.pdf
Appears in Collections:Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά)

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