Isolation of a cDNA clone for the acyl carrier protein-I of spinach

A 715 base pair cDNA clone coding for an acyl carrier protein (ACP) in spinach leaves has been isolated and characterized. The amino acid sequence indicated by the cDNA sequence closely matches the amino acid sequence of the ACP-I isoform. The presence of polyadenylation and DNA sequence coding for...

Full description

Saved in:
Bibliographic Details
Published inPlant molecular biology Vol. 9; no. 2; pp. 127 - 134
Main Authors Scherer, D.E, Knauf, V.C
Format Journal Article
LanguageEnglish
Published Netherlands 01.01.1987
Subjects
amino acid sequences
cloning
DNA
gene expression
genes
messenger RNA
molecular sequence data
nucleotide sequences
plant proteins
restriction mapping
Spinacia oleracea
Online AccessGet more information

Cover

More Information
Summary:A 715 base pair cDNA clone coding for an acyl carrier protein (ACP) in spinach leaves has been isolated and characterized. The amino acid sequence indicated by the cDNA sequence closely matches the amino acid sequence of the ACP-I isoform. The presence of polyadenylation and DNA sequence coding for a precursor protein with a putative transit peptide, and the absence of hybridization between the cloned DNA and isolated spinach plastid DNA collectively show that the ACP-I gene is nuclear-encoded. The ACP-I cloned DNA did not cross-hybridize with mRNA from spinach tissues in which Acp-II has been found. Cross-hybridization with mRNA from tissues of Brassica campestris was either weak or undetectable. The cloning of an ACP-I gene represents an initial step in the molecular dissection of fatty acid synthetase in plants.
ISSN:0167-4412
1573-5028
DOI:10.1007/BF00015645