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THE PLANT CELL, Vol 8, Issue 11 2105-2115, Copyright © 1996 by American Society of Plant Biologists
MFP1, a Novel Plant Filament-like Protein with Affinity for Matrix Attachment Region DNA
I. Meier, T. Phelan, W. Gruissem, S. Spiker and D. Schneider
Institute for General Botany, Applied Molecular Biology of Plants I, University of Hamburg, Ohnhorststrasse 18, D-22609 Hamburg, Germany
The interaction of chromatin with the nuclear matrix via matrix attachment
regions (MARs) on the DNA is considered to be of fundamental importance for
higher order chromatin organization and regulation of gene expression.
Here, we report a novel nuclear matrix-localized MAR DNA binding protein,
designated MAR binding filament-like protein 1 (MFP1), from tomato. In
contrast to the few animal MAR DNA binding proteins thus far identified,
MFP1 contains a predicted N-terminal transmembrane domain and a long
filament-like [alpha]-helical domain that is similar to diverse nuclear and
cytoplasmic filament proteins from animals and yeast. DNA binding assays
established that MFP1 can discriminate between animal and plant MAR DNAs
and non-MAR DNA fragments of similar size and AT content. Deletion mutants
of MFP1 revealed a novel, discrete DNA binding domain near the C terminus
of the protein. MFP1 is an in vitro substrate for casein kinase II, a
nuclear matrix-associated protein kinase. Its structure, MAR DNA binding
activity, and nuclear matrix localization suggest that MFP1 is likely to
participate in nuclear architecture by connecting chromatin with the
nuclear matrix and potentially with the nuclear envelope.
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