RT Journal Article
SR Electronic
T1 MAF1, a Novel Plant Protein Interacting with Matrix Attachment Region Binding Protein MFP1, Is Located at the Nuclear Envelope
JF The Plant Cell
JO Plant Cell
FD American Society of Plant Biologists
SP 1755
OP 1767
DO 10.1105/tpc.11.9.1755
VO 11
IS 9
A1 Gindullis, Frank
A1 Peffer, Nancy J.
A1 Meier, Iris
YR 1999
UL http://www.plantcell.org/content/11/9/1755.abstract
AB The interaction of chromatin with the nuclear matrix via matrix attachment region (MAR) DNA is considered to be of fundamental importance for chromatin organization in all eukaryotic cells. MAR binding filament–like protein 1 (MFP1) from tomato is a novel plant protein that specifically binds to MAR DNA. Its filament protein–like structure makes it a likely candidate for a structural component of the nuclear matrix. MFP1 is located at nuclear matrix–associated, specklelike structures at the nuclear envelope. Here, we report the identification of a novel protein that specifically interacts with MFP1 in yeast two-hybrid and in vitro binding assays. MFP1 associated factor 1 (MAF1) is a small, soluble, serine/threonine-rich protein that is ubiquitously expressed and has no similarity to known proteins. MAF1, like MFP1, is located at the nuclear periphery and is a component of the nuclear matrix. These data suggest that MFP1 and MAF1 are in vivo interaction partners and that both proteins are components of a nuclear substructure, previously undescribed in plants, that connects the nuclear envelope and the internal nuclear matrix.