|
PLANT PHYSIOLOGY , Vol 106, Issue 4 1593-1604, Copyright © 1994 by American Society of Plant Biologists
|
MOLECULAR BIOLOGY AND GENE REGULATION |
Two Genes Encoding GF14 (14-3-3) Proteins in Zea mays (Structure, Expression, and Potential Regulation by the G-Box-Binding Complex)
N. C. de Vetten and R. J. Ferl
Department of Horticultural Sciences, Program in Plant Molecular and Cellular Biology, 1243 Fifield Hall, University of Florida, Gainesville, Florida 32611
Two maize (Zea mays) genes, designated GRF1 and GRF2, have been isolated
and characterized. The proteins encoded by these genes, called GF14
proteins, participate in protein/DNA complexes and show more than 60%
identity with a highly conserved, widely distributed protein family,
collectively referred to as 14-3-3 proteins. Members of the 14-3-3 protein
family have been reported to activate Tyr and Trp hydroxylases, modulate
protein kinase C activity, and activate ADP-ribosyltransferase. The mRNAs
of the GRF genes are encoded by six exons interrupted by five introns. The
transcriptional units of the GRF genes were found to be very similar, with
complete conservation of the intron positions. In addition, the length and
nucleotide sequences of the two genes' introns were highly conserved. The
5[prime] flanking sequences of the two GRF genes were compared and regions
of homology and divergence identified. This comparison revealed the
presence of a conserved G-box element in the 5[prime] flanking region of
both genes. Electrophoretic mobility shift assays of maize protein extract
with the GRF G-box indicates that GBF binds to this G-box site in the
5[prime] upstream region of GRF. Antibody supershifts indicate that GF14
protein is associated with the G-box-binding complex that interacts with
the GRF upstream region.
This article has been cited by other articles:
|
|
|
|
 
A.-L. Paul, P. C. Sehnke, and R. J. Ferl
Isoform-specific Subcellular Localization among 14-3-3 Proteins in Arabidopsis Seems to be Driven by Client Interactions
Mol. Biol. Cell,
April 1, 2005;
16(4):
1735 - 1743.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
S. Comparot, G. Lingiah, and T. Martin
Function and specificity of 14-3-3 proteins in the regulation of carbohydrate and nitrogen metabolism
J. Exp. Bot.,
January 3, 2003;
54(382):
595 - 604.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. Datta, K. C. Chamusco, and P. S. Chourey
Starch Biosynthesis during Pollen Maturation Is Associated with Altered Patterns of Gene Expression in Maize
Plant Physiology,
December 1, 2002;
130(4):
1645 - 1656.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
P. C. Sehnke, J. M. DeLille, and R. J. Ferl
Consummating Signal Transduction: The Role of 14-3-3 Proteins in the Completion of Signal-Induced Transitions in Protein Activity
PLANT CELL,
May 1, 2002;
14(90001):
S339 - 354.
[Full Text]
[PDF]
|
|
|
|
|
|
|
P. C. Sehnke, H.-J. Chung, K. Wu, and R. J. Ferl
Regulation of starch accumulation by granule-associated plant 14-3-3 proteins
PNAS,
January 5, 2001;
(2001)
21304198.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
S. Pan, P. C. Sehnke, R. J. Ferl, and W. B. Gurley
Specific Interactions with TBP and TFIIB in Vitro Suggest That 14-3-3 Proteins May Participate in the Regulation of Transcription When Part of a DNA Binding Complex
PLANT CELL,
August 1, 1999;
11(8):
1591 - 1602.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
M. R. Fullone, S. Visconti, M. Marra, V. Fogliano, and P. Aducci
Fusicoccin Effect on the in Vitro Interaction between Plant 14-3-3 Proteins and Plasma Membrane H+-ATPase
J. Biol. Chem.,
March 27, 1998;
273(13):
7698 - 7702.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
P. C. Sehnke, H.-J. Chung, K. Wu, and R. J. Ferl
Regulation of starch accumulation by granule-associated plant 14-3-3 proteins
PNAS,
January 16, 2001;
98(2):
765 - 770.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
