caa a22 4500 467893926 CHVBK 20180406152757.0 cr unu---uuuuu 170328e20060301xx s 000 0 eng 10.1007/s11103-005-5471-1 doi (NATIONALLICENCE)springer-10.1007/s11103-005-5471-1 Shimomura Shoji Department of Biochemistry, National Institute of Agrobiological Sciences, Kannondai 2-1-2, 305-8602, Tsukuba, Ibaraki, Japan aut Identification of a Glycosylphosphatidylinositol-anchored Plasma Membrane Protein Interacting with the C-terminus of Auxin-binding Protein 1: A Photoaffinity Crosslinking Study [Elektronische Daten] [Shoji Shimomura] Synthetic peptides corresponding to the C-terminus of auxin-binding protein 1 (ABP1) have been shown to function as auxin agonists. To define a C-terminal receptor, photoaffinity crosslinking experiments were performed using an azido derivative of a C-terminal peptide and plasma membranes from maize (Zea mays L.). The crosslinking reaction was monitored by immunoblotting using anti-ABP1 antibodies. The crosslinked proteins were isolated by 2D gel electrophoresis and identified by mass spectrometric analysis. Further, the noncrosslinked forms of these proteins were also identified. Two proteins with apparent molecular masses of 73kDa (termed C-terminal peptide-binding protein 1, CBP1) and 35kDa (CBP2) were specifically linked with the C-terminal peptide. CBP2 is a cytoplasmic protein that consists of two conserved domains that are characteristic of a ricin-type lectin domain. CBP2 remained in the detergent-insoluble particles and was released from the particles by the addition of monosaccharides such as methyl-β-d-galactopyranoside. CBP1 was released from the membranes by treatment with phosphatidylinositol-specific phospholipase C, indicating that CBP1 is a glycosylphosphatidylinositol (GPI)-anchored plasma membrane protein. CBP1 was found to be a copper-binding protein, and is highly homologous to Arabidopsis thaliana SKU5 that contributes to directional root growth processes. Further, it is similar to A. thaliana SKS6 that contributes to cotyledon vascular patterning and to Nicotiana tabacum NTP303 that contributes to pollen tube growth. The present results indicate that ABP1 may contribute to directional cell growth processes via the GPI-anchored plasma membrane protein SKU5 and its family members. Springer, 2006 auxin-binding protein nationallicence cell elongation nationallicence docking protein nationallicence glycosylphosphatidylinositol anchor nationallicence multicopper oxidase nationallicence photoaffinity crosslinking nationallicence ABP1 : auxin-binding protein 1 nationallicence BSA : bovine serum albumin nationallicence CBB : Coomassie brilliant blue nationallicence CBP : C-terminal peptide-binding protein nationallicence CHAPS : 3-[(3-cholamidopropyl) dimethylammonio] propanesulfonic acid nationallicence CL-CBP : crosslinked product of CBP nationallicence GF-AAS : graphite furnace atomic absorption spectrometry nationallicence GPI : glycosylphosphatidylinositol nationallicence MBP : maltose-binding protein nationallicence PAGE : polyacrylamide gel electrophoresis nationallicence PI-PLC : phosphatidylinositol-specific phospholipase C nationallicence PVDF : polyvinylidene difluoride nationallicence Plant Molecular Biology Kluwer Academic Publishers 60/5(2006-03-01), 663-677 0167-4412 60:5<663 2006 60 11103 https://doi.org/10.1007/s11103-005-5471-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11103-005-5471-1 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- Shimomura Shoji Department of Biochemistry, National Institute of Agrobiological Sciences, Kannondai 2-1-2, 305-8602, Tsukuba, Ibaraki, Japan aut NATIONALLICENCE 773 0- Plant Molecular Biology Kluwer Academic Publishers 60/5(2006-03-01), 663-677 0167-4412 60:5<663 2006 60 11103 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer