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PMID: 10715321 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

A conserved domain of the arabidopsis GNOM protein mediates subunit interaction and cyclophilin 5 binding.

The Plant cell ·Vol. 12 ·No. 3 ·2000-03-00 ·Pages 343-56

Grebe M, Gadea J, Steinmann T, Kientz M, Rahfeld JU, Salchert K, Koncz C, Jürgens G

Abstract

The Arabidopsis GNOM protein, a guanine nucleotide exchange factor (GEF) that acts on ADP ribosylation factor (ARF)-type G proteins, is required for coordination of cell polarity along the apical-basal embryo axis. Interallelic complementation of gnom mutants suggested that dimerization is involved in GNOM function. Here, direct interaction between GNOM molecules is demonstrated in vitro and by using a yeast two-hybrid system. Interaction was confined to an N-terminal domain conserved within a subgroup of large ARF GEFs. The same domain mediated in vitro binding to cyclophilin 5 (Cyp5), which was identified as a GNOM interactor in two-hybrid screening. Cyp5 displayed peptidylprolyl cis/trans-isomerase and protein refolding activities that were sensitive to cyclosporin A. Cyp5 protein accumulated in several plant organs and, like GNOM, was partitioned between cytosolic and membrane fractions. Cyp5 protein was also expressed in the developing embryo. Our results suggest that Cyp5 may regulate the ARF GEF function of the GNOM protein during embryogenesis.

MeSH Terms
ADP-Ribosylation Factors/chemistry,genetics Amino Acid Sequence Arabidopsis/embryology,genetics,metabolism Binding Sites Catalysis/drug effects Conserved Sequence Cyclosporine/pharmacology Dimerization Guanine Nucleotide Exchange Factors/chemistry,genetics,metabolism Molecular Sequence Data Peptidylprolyl Isomerase/genetics,isolation & purification,metabolism Plant Proteins/chemistry,genetics,metabolism Protein Binding Protein Folding Protein Structure, Tertiary Recombinant Fusion Proteins/genetics,metabolism Seeds/growth & development,metabolism Sequence Homology, Amino Acid Two-Hybrid System Techniques
Chemicals
Guanine Nucleotide Exchange Factors Plant Proteins Recombinant Fusion Proteins Cyclosporine ADP-Ribosylation Factors Peptidylprolyl Isomerase
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Grebe M
Entwicklungsgenetik, Zentrum für Molekularbiologie der Pflanzen, Universität Tübingen, Auf der Morgenstelle 1, D-72076 Tübingen, Germany.
Gadea J
Steinmann T
Kientz M
Rahfeld J U
Salchert K
Koncz C
Jürgens G
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Article Info
Journal
The Plant cell
Abbr.
Plant Cell
ISSN
1040-4651
DOI
10.1105/tpc.12.3.343
Published
2000-03-00
Pages
343-56
Language
English
Region
England
NLM ID
9208688
PMCID
PMC139835
Subset
IM
External Links
PubMed source DOI: 10.1105/tpc.12.3.343 PMC Full Text View journal details
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