|
Plant Physiol, January 2000, Vol. 122, pp. 225-234
Conservation of Matrix Attachment Region-Binding
Filament-Like Protein 1 among Higher Plants1
Patricia A.
Harder,
Rebecca A.
Silverstein,2 and
Iris
Meier*
DuPont Central Research and Development, P.O. Box 80402, Wilmington, Delaware 19880-0402 (P.A.H.); Applied Plant Molecular
Biology I, University of Hamburg, Ohnhorststrasse 18, D-22609 Hamburg,
Germany (R.A.S., I.M.); and Department of Plant Biology, Ohio State
University, 1060 Carmack Road, Columbus, Ohio 43210 (I.M.).
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 the regulation of gene
expression. We have previously isolated a novel nuclear
matrix-localized protein (MFP1) from tomato (Lycopersicon esculentum) that preferentially binds to MAR DNA. Tomato MFP1 has a predicted filament-protein-like structure and is associated with
the nuclear envelope via an N-terminal targeting domain. Based on the
antigenic relationship, we report here that MFP1 is conserved in a
large number of dicot and monocot species. Several cDNAs were cloned
from tobacco (Nicotiana tabacum) and shown to correspond
to two tobacco MFP1 genes. Comparison of the primary and predicted
secondary structures of MFP1 from tomato, tobacco, and Arabidopsis
indicates a high degree of conservation of the N-terminal targeting
domain, the overall putative coiled-coil structure of the protein, and
the C-terminal DNA-binding domain. In addition, we show that tobacco
MFP1 is regulated in an organ-specific and developmental fashion, and
that this regulation occurs at the level of transcription or RNA stability.
1
This work was supported in part by the German
Science Foundation (grant no. ME 1133/2-1 to I.M.).
2
Present address: Centrum för Bioteknik,
NOVUM, 14157 Huddinge, Sweden.
*
Corresponding author; e-mail meier.56{at}osu.edu; fax
614-292-6345.
© 2000 American Society of Plant Physiologists
This article has been cited by other articles:
|
|
|
|
 
R. Samaniego, S. Y. Jeong, C. de la Torre, I. Meier, and S. M. Diaz de la Espina
CK2 phosphorylation weakens 90 kDa MFP1 association to the nuclear matrix in Allium cepa
J. Exp. Bot.,
January 1, 2006;
57(1):
113 - 124.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
T. CAVALIER-SMITH
Economy, Speed and Size Matter: Evolutionary Forces Driving Nuclear Genome Miniaturization and Expansion
Ann. Bot.,
January 1, 2005;
95(1):
147 - 175.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Rudd, M. Frisch, K. Grote, B. C. Meyers, K. Mayer, and T. Werner
Genome-Wide in Silico Mapping of Scaffold/Matrix Attachment Regions in Arabidopsis Suggests Correlation of Intragenic Scaffold/Matrix Attachment Regions with Gene Expression
Plant Physiology,
June 1, 2004;
135(2):
715 - 722.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Rose, S. Manikantan, S. J. Schraegle, M. A. Maloy, E. A. Stahlberg, and I. Meier
Genome-Wide Identification of Arabidopsis Coiled-Coil Proteins and Establishment of the ARABI-COIL Database
Plant Physiology,
March 1, 2004;
134(3):
927 - 939.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Y. Jeong, A. Rose, and I. Meier
MFP1 is a thylakoid-associated, nucleoid-binding protein with a coiled-coil structure
Nucleic Acids Res.,
September 1, 2003;
31(17):
5175 - 5185.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. Rose, F. Gindullis, and I. Meier
A novel alpha-helical protein, specific to and highly conserved in plants, is associated with the nuclear matrix fraction
J. Exp. Bot.,
April 1, 2003;
54(385):
1133 - 1141.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Fujiwara, N. Matsuda, T. Sato, S. Sonobe, and M. Maeshima
Molecular Properties of a Matrix Attachment Region-Binding Protein Located in the Nucleoli of Tobacco Cells
Plant Cell Physiol.,
December 15, 2002;
43(12):
1558 - 1567.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
