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rdf:type |
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lifeskim:mentions |
umls-concept:C0022660,
umls-concept:C0061928,
umls-concept:C0080347,
umls-concept:C0205369,
umls-concept:C0525037,
umls-concept:C0969730,
umls-concept:C1148642,
umls-concept:C1335223,
umls-concept:C1419277,
umls-concept:C1511359,
umls-concept:C1514562,
umls-concept:C1705280,
umls-concept:C1825810,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2827404
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pubmed:issue |
6
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pubmed:dateCreated |
2001-1-30
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pubmed:databankReference |
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pubmed:abstractText |
Arabidopsis proteins were predicted which share an 80 residue zinc finger domain known from ADP-ribosylation factor GTPase-activating proteins (ARF GAPs). One of these is a 37 kDa protein, designated ZAC, which has a novel domain structure in which the N-terminal ARF GAP domain and a C-terminal C2 domain are separated by a region without homology to other known proteins. Zac promoter/beta-glucuronidase reporter assays revealed highest expression levels in flowering tissue, rosettes and roots. ZAC protein was immuno-detected mainly in association with membranes and fractionated with Golgi and plasma membrane marker proteins. ZAC membrane association was confirmed in assays by a fusion between ZAC and the green fluorescence protein and prompted an analysis of the in vitro phospholipid-binding ability of ZAC. Phospholipid dot-blot and liposome-binding assays indicated that fusion proteins containing the ZAC-C2 domain bind anionic phospholipids non-specifically, with some variance in Ca2+ and salt dependence. Similar assays demonstrated specific affinity of the ZAC N-terminal region (residues 1-174) for phosphatidylinositol 3-monophosphate (PI-3-P). Binding was dependent in part on an intact zinc finger motif, but proteins containing only the zinc finger domain (residues 1-105) did not bind PI-3-P. Recombinant ZAC possessed GTPase-activating activity on Arabidopsis ARF proteins. These data identify a novel PI-3-P-binding protein region and thereby provide evidence that this phosphoinositide is recognized as a signal in plants. A role for ZAC in the regulation of ARF-mediated vesicular transport in plants is discussed.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0167-4412
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
44
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
799-814
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11202441-ADP-Ribosylation Factors,
pubmed-meshheading:11202441-Amino Acid Sequence,
pubmed-meshheading:11202441-Arabidopsis,
pubmed-meshheading:11202441-Binding, Competitive,
pubmed-meshheading:11202441-Binding Sites,
pubmed-meshheading:11202441-DNA, Complementary,
pubmed-meshheading:11202441-Expressed Sequence Tags,
pubmed-meshheading:11202441-GTPase-Activating Proteins,
pubmed-meshheading:11202441-Gene Expression,
pubmed-meshheading:11202441-Membrane Proteins,
pubmed-meshheading:11202441-Molecular Sequence Data,
pubmed-meshheading:11202441-Phospholipids,
pubmed-meshheading:11202441-Protein Binding,
pubmed-meshheading:11202441-RNA, Messenger,
pubmed-meshheading:11202441-Recombinant Fusion Proteins,
pubmed-meshheading:11202441-Sequence Alignment,
pubmed-meshheading:11202441-Sequence Analysis, DNA,
pubmed-meshheading:11202441-Sequence Homology, Amino Acid,
pubmed-meshheading:11202441-Tissue Distribution,
pubmed-meshheading:11202441-Zinc Fingers
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pubmed:year |
2000
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pubmed:articleTitle |
Promiscuous and specific phospholipid binding by domains in ZAC, a membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a C2 domain.
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pubmed:affiliation |
Institute of Molecular Biology, University of Copenhagen, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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