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一种存在于前体积累小泡中的南瓜72-kDa膜蛋白具有液泡分选受体的特征。

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

作者信息

Shimada T, Kuroyanagi M, Nishimura M, Hara-Nishimura I

机构信息

Department of Cell Biology, National Institute for Basic Biology, Okazaki, Japan.

出版信息

Plant Cell Physiol. 1997 Dec;38(12):1414-20. doi: 10.1093/oxfordjournals.pcp.a029138.

Abstract

Precursor-accumulating (PAC) vesicles were previously shown to mediate the transport of the precursor of a major storage protein (pro2S albumin) to protein-storage vacuoles 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.

摘要

先前的研究表明,前体积累(PAC)囊泡可介导一种主要储存蛋白(pro2S白蛋白)的前体向发育中的南瓜子叶中的蛋白储存液泡运输。在本研究中,我们鉴定了PAC囊泡中的两种同源蛋白,一种72 kDa蛋白(PV72)和一种82 kDa蛋白(PV82)。PV72和PV82显示出与来自pro2S白蛋白内部前肽和C端肽的肽结合的能力。PV72被预测为具有表皮生长因子(EGF)样基序的I型整合膜蛋白。这些结果表明,PV72和PV82是2S白蛋白向蛋白储存液泡的潜在分选受体。

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