Large alkyl side-chains of isoleucine and leucine in the NPIRL region constitute the core of the vacuolar sorting determinant of sporamin precursor

被引：49

作者：

Matsuoka, K ^{[1
]}

Nakamura, K ^{[1
]}

机构：

[1] Nagoya Univ, Grad Sch Bioagr Sci, Biochem Lab, Chikusa Ku, Nagoya, Aichi 4648601, Japan

来源：

PLANT MOLECULAR BIOLOGY | 1999年 / 41卷 / 06期

关键词：

hydrophobic interaction; N-terminal propeptide; protein sorting; secretory pathway; targeting signal; vacuole;

D O I：

10.1023/A:1006357413084

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The N-terminal propeptide of the sporamin precursor contains vacuolar targeting information within the Asn-26/Pro-27/Ile-28/Arg-29/Leu-30 (NPIRL) sequence. An Agrobacterium-mediated transient expression assay with tobacco BY-2 cells was employed to investigate the role of each amino acid of the NPIRL region in vacuolar targeting. Replacement of Asn-26, Pro-27, Ile-28 and Leu-30 with several amino acids caused secretion of the mutant prosporamin. Leu was the only amino acid that could be substituted for Ile-28 without affecting transport. Exchange of Leu-30 for amino acids with small side-chains abolished vacuolar delivery. These results indicate that the consensus composition of the NPIRL sequence is [preferably Asn]-[not acidic]-[Ile or Leu]-[any amino acid]-[large and hydrophobic] and suggest that the large alkyl side-chains of Ile-28 and Leu-30 constitute the core of the vacuolar sorting determinant.

引用

页码：825 / 835

页数：11

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