The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants - PubMed (original) (raw)

The barley lectin carboxyl-terminal propeptide is a vacuolar protein sorting determinant in plants

S Y Bednarek et al. Plant Cell. 1991 Nov.

Abstract

We have previously shown that the 15-amino acid carboxyl-terminal propeptide of probarley lectin is necessary for the proper sorting of this protein to the plant vacuole. A mutant form of the protein lacking the carboxyl-terminal propeptide is secreted. To test whether the carboxyl-terminal propeptide is the vacuole sorting determinant of probarley lectin, we examined in transgenic tobacco the processing and sorting of a series of fusion proteins containing the secreted protein, cucumber chitinase, and regions of probarley lectin. Pulse-labeling experiments demonstrated that the fusion proteins were properly translocated through the tobacco secretory system and that cucumber chitinase and cucumber chitinase fusion proteins lacking the carboxyl-terminal propeptide were secreted. The cucumber chitinase fusion protein containing the carboxyl-terminal propeptide was properly processed and sorted to the vacuole in transgenic tobacco as confirmed by organelle fractionation and electron microscopy immunocytochemistry. Therefore, the barley lectin carboxyl-terminal propeptide is both necessary and sufficient for protein sorting to the plant vacuole.

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References

    1. Cell. 1987 Aug 14;50(4):521-2 - PubMed
    1. Proc Natl Acad Sci U S A. 1989 Apr;86(8):2673-7 - PubMed
    1. Biochemistry. 1984 Jan 17;23(2):280-7 - PubMed
    1. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1496-500 - PubMed
    1. Proc Natl Acad Sci U S A. 1991 Feb 1;88(3):834-8 - PubMed

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