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PMID: 9056226 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

The heterologous interactions among plant 14-3-3 proteins and identification of regions that are important for dimerization.

Archives of biochemistry and biophysics ·Vol. 339 ·No. 1 ·1997-03-01 ·Pages 2-8

Wu K, Lu G, Sehnke P, Ferl RJ

Abstract

The 14-3-3 proteins constitute a family of dimeric proteins that are involved in many cellular functions. At least two mammalian 14-3-3 proteins can form heterodimers and the approximate regions important for dimerization have been identified. In this study, we demonstrate that eight Arabidopsis and one maize 14-3-3 protein can dimerize with each other and with themselves. Native gel Western analysis of Arabidopsis cell extract also suggests the presence of 14-3-3 heterodimers in vivo. Finally, we identified the domains of one 14-3-3 protein that are sufficient for homodimerization and heterodimerization. These data support the hypothesis that evolutionarily divergent 14-3-3 proteins can interact with each other to form diverse molecular modulators or adapters in signaling pathways.

MeSH Terms
14-3-3 Proteins Amino Acid Sequence Arabidopsis/chemistry Blotting, Western Molecular Sequence Data Molecular Weight Plant Proteins/chemistry Protein Binding Proteins/chemistry Recombinant Proteins Saccharomyces cerevisiae Sequence Alignment Sequence Homology, Amino Acid Structure-Activity Relationship Tyrosine 3-Monooxygenase Zea mays/chemistry
Chemicals
14-3-3 Proteins Plant Proteins Proteins Recombinant Proteins Tyrosine 3-Monooxygenase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Wu K
Horticultural Science Department, University of Florida, Gainesville 32611, USA.
Lu G
Sehnke P
Ferl R J
Article Info
Journal
Archives of biochemistry and biophysics
Abbr.
Arch Biochem Biophys
ISSN
0003-9861
Published
1997-03-01
Pages
2-8
Language
English
Region
United States
NLM ID
0372430
Subset
IM
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