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Molecular cloning of cDNA encoding potato amyloplast alpha-glucan phosphorylase and the structure of its transit peptide.

Authors
Type
Published Article
Journal
Journal of biochemistry
Publication Date
Volume
106
Issue
4
Pages
691–695
Identifiers
PMID: 2481677
Source
Medline
License
Unknown

Abstract

The type L isozyme of potato tuber alpha-glucan phosphorylase [EC 2.4.1.1], a dimer of 104-kDa subunits, is compartmentalized in the amyloplast. We have cloned a nearly full-length cDNA encoding this isozyme from a cDNA library of immature potato tuber. The sequence was supplemented by a partial genomic clone. The transcription initiation site was identified by a primer extension experiment to be 43 bases upstream from the translation initiation ATG codon. The message encodes a polypeptide of 966 amino acid residues, of which 50 residues constitute an N-terminal extended peptide and 916 residues make up the mature protein. In the mature protein region, the nucleotide sequence is consistent with the chemically determined amino acid sequence (Nakano, K. & Fukui, T. (1986) J. Biol. Chem. 261, 8230-8236). The N-terminal extension bears characteristic features of the transit peptides of nuclear-encoded chloroplastic proteins, and is therefore regarded as a transit peptide for the amyloplast. This peptide is rich in basic amino acids (5 arginines, 3 lysines, and 5 histidines) and hydroxylic amino acids (7 serines and 5 threonines), but lacks acidic amino acids. It is therefore classified as one of the most basic transit peptides so far reported.

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