Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Promiscuous and specific phospholipid binding by domains in ZAC, a membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a C2 domain
Autore:
Jensen, RB; Lykke-Andersen, K; Frandsen, GI; Nielsen, HB; Haseloff, J; Jespersen, HM; Mundy, J; Skriver, K;
Indirizzi:
Univ Copenhagen, Inst Mol Biol, DK-1353 Copenhagen K, Denmark Univ Copenhagen Copenhagen Denmark K Biol, DK-1353 Copenhagen K, Denmark Univ Cambridge, Dept Plant Sci, Cambridge CB2 3EA, England Univ CambridgeCambridge England CB2 3EA Sci, Cambridge CB2 3EA, England
Titolo Testata:
PLANT MOLECULAR BIOLOGY
fascicolo: 6, volume: 44, anno: 2000,
pagine: 799 - 814
SICI:
0167-4412(200012)44:6<799:PASPBB>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; ADP-RIBOSYLATION FACTOR; GUANINE-NUCLEOTIDE-EXCHANGE; C-2 DOMAIN; SYNAPTOTAGMIN; LOCALIZATION; THALIANA; CLONING; FAMILY; HYDROLYSIS;
Keywords:
Arabidopsis thaliana; ARF GAP; C2 domain; phosphoinositide binding; phospholipid binding; zinc finger;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Skriver, K Univ Copenhagen, Inst Mol Biol, Oster Farimagsgade 2A, DK-1353 Copenhagen K, Denmark Univ Copenhagen Oster Farimagsgade 2A Copenhagen Denmark K ark
Citazione:
R.B. Jensen et al., "Promiscuous and specific phospholipid binding by domains in ZAC, a membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a C2 domain", PLANT MOL B, 44(6), 2000, pp. 799-814

Abstract

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 andplasma membrane marker proteins. ZAC membrane association was confirmed inassays 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 proteinscontaining the ZAC-C2 domain bind anionic phospholipids non-specifically, with some variance in Ca2+ and salt dependence. Similar assays demonstratedspecific 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 07:51:52