Linked Life Data

2481677

Source:http://linkedlifedata.com/resource/pubmed/id/2481677

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-2-22
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
106
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
691-5
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Molecular cloning of cDNA encoding potato amyloplast alpha-glucan phosphorylase and the structure of its transit peptide.
pubmed:affiliation
Institute of Scientific and Industrial Research, Osaka University.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't