A pumpkin [Cucurbita sp.] 72-kDa membrane protein of precursor-accumulating vesicles has characteristics of a vacuolar sorting receptor

Precursor-accumulating (PAC) vesicles were previously shown to mediate the transport of the precursor of a major storage protein (pro2S albumin) to protein-storage vacu-oles in developing pumpkin cotyledons. In this study, we characterized two homologous proteins from PAC vesicles, a 72 kDa protein...

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Veröffentlicht in:Plant and cell physiology 1997-12, Vol.38 (12), p.1414-1420
Hauptverfasser: Shimada, T. (National Inst. for Basic Biology, Okazaki, Aichi (Japan)), Kuroyanagi, M, Nishimura, M, Nishimura, I.H
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Sprache:eng
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Zusammenfassung:Precursor-accumulating (PAC) vesicles were previously shown to mediate the transport of the precursor of a major storage protein (pro2S albumin) to protein-storage vacu-oles in developing pumpkin cotyledons. In this study, we characterized two homologous proteins from PAC vesicles, a 72 kDa protein (PV72) and an 82 kDa protein (PV82). PV72 and PV82 showed an ability to bind to peptides derived from both an internal propeptide and a C-terminal peptide of pro2S albumin. PV72 was predicted to be a type I integral membrane protein with epidermal growth factor (EGF)-like motifs. These results suggest that PV72 and PV82 are potential sorting receptors for 2S albumin to protein-storage vacuoles.
ISSN:0032-0781
1471-9053
DOI:10.1093/oxfordjournals.pcp.a029138