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PMID: 9596641 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

14-3-3 proteins are part of an abscisic acid-VIVIPAROUS1 (VP1) response complex in the Em promoter and interact with VP1 and EmBP1.

The Plant cell ·Vol. 10 ·No. 5 ·1998-05-00 ·Pages 837-47

Schultz TF, Medina J, Hill A, Quatrano RS

Abstract

Protein-DNA complexes were formed when nuclear extracts from embryogenic rice suspension cultures or maize embryos were incubated with an abscisic acid-VIVIPAROUS1 (VP1) response element (Em1a) from the Em promoter. Monoclonal antibodies generated to GF14, a 14-3-3 protein from plants, resulted in gel retardation of the Em1a-protein complexes. Antibodies generated to the C and N termini of GF14 detected protein isoforms in rice nuclear and cytoplasmic extracts, but no differences in distribution of the GF14 isoforms were recognized between the nucleus and cytoplasm or when abscisic acid-treated and untreated tissues were compared. When recombinant GF14 fusion proteins from rice were added to nuclear extracts, novel complexes were formed that required the dimerization domain of GF14. Chemical cross-linking showed that GF-14 interacted with the basic leucine zipper factor EmBP1, which binds specifically to Em1a, and with VP1, which transactivates Em through Em1a. GF14 proteins from rice were shown to interact with VP1 in yeast through the dimerization domain of GF14. Our results indicated that GF14 interacts with both site-specific DNA binding proteins (i.e., EmBP1) and tissue-specific regulatory factors (i.e., VP1) and may provide a structural link between VP1 and the Em1a transcriptional complex.

MeSH Terms
14-3-3 Proteins Abscisic Acid/metabolism Amino Acid Sequence Animals Antibodies, Monoclonal/pharmacology Cell Nucleus/metabolism Cloning, Molecular DNA, Plant/metabolism DNA-Binding Proteins/metabolism Dimerization Leucine Zippers Molecular Sequence Data Oryza/genetics,metabolism Plant Proteins Promoter Regions, Genetic Proteins/chemistry,metabolism Recombinant Proteins/chemistry,metabolism Saccharomyces cerevisiae Sequence Alignment Sequence Homology, Amino Acid Sheep Trans-Activators Transcription Factors/metabolism Transcriptional Activation Tyrosine 3-Monooxygenase Zea mays/genetics,metabolism
Chemicals
14-3-3 Proteins Antibodies, Monoclonal DNA, Plant DNA-Binding Proteins Plant Proteins Proteins Recombinant Proteins Trans-Activators Transcription Factors Abscisic Acid Tyrosine 3-Monooxygenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schultz T F
Department of Biology and Curriculum in Genetics and Molecular Biology, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-3280, USA.
Medina J
Hill A
Quatrano R S
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Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
DOI
10.1105/tpc.10.5.837
Published
1998-05-00
Pages
837-47
Language
English
Region
England
NLM ID
9208688
PMCID
PMC144375
Subset
IM
Grants
NIGMS NIH HHS · GM 13588 · United States
NIGMS NIH HHS · GM 44288 · United States
External Links
PubMed source DOI: 10.1105/tpc.10.5.837 PMC Full Text View journal details
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