Abstract
The interactions of nuclear lamins with the chromatin fiber play an important role in regulating nuclear architecture and chromatin function; however, the full spectrum of these interactions is not known. We report that the N-terminal domain of the nucleosome-binding protein HMGN5 interacts with the C-terminal domain of the lamin-binding protein LAP2α and that these proteins reciprocally alter their interaction with chromatin. Chromatin immunoprecipitation analysis of cells lacking either HMGN5 or LAP2α reveals that loss of either protein affects the genome-wide distribution of the remaining partner. Our study identifies a new functional link between chromatin-binding and lamin-binding proteins.
Keywords:
Cell Biology; Chromatin; Chromosomes/Non-histone Chromosomal Proteins; HMG Proteins; LAP2Alpha; Lamin; Nuclear Organization.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, N.I.H., Intramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Binding Sites / genetics
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Blotting, Western
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Cell Nucleus / metabolism
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Chromatin / genetics
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Chromatin / metabolism*
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Chromatin Immunoprecipitation
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism*
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Fluorescence Recovery After Photobleaching
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Genome, Human*
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HEK293 Cells
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HMGN Proteins / genetics
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HMGN Proteins / metabolism*
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HeLa Cells
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Humans
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Kinetics
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Luminescent Proteins / genetics
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Luminescent Proteins / metabolism
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Protein Binding
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RNA Interference
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Trans-Activators / genetics
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Trans-Activators / metabolism*
Substances
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Chromatin
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DNA-Binding Proteins
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HMGN Proteins
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HMGN5 protein, human
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Luminescent Proteins
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Membrane Proteins
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Trans-Activators
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lamina-associated polypeptide 2