Isolation of a Cdna Clone for Spinach Lipid Transfer Protein and Evidence That the Protein Is Synthesized by the Secretory Pathway

Bernhard, WR, Thoma, S, Botella, J and Somerville, CR (1991) Isolation of a Cdna Clone for Spinach Lipid Transfer Protein and Evidence That the Protein Is Synthesized by the Secretory Pathway. Plant Physiology, 95 1: 164-170. doi:10.1104/pp.95.1.164


Author Bernhard, WR
Thoma, S
Botella, J
Somerville, CR
Title Isolation of a Cdna Clone for Spinach Lipid Transfer Protein and Evidence That the Protein Is Synthesized by the Secretory Pathway
Journal name Plant Physiology   Check publisher's open access policy
ISSN 0032-0889
Publication date 1991-01-01
Year available 1991
Sub-type Article (original research)
DOI 10.1104/pp.95.1.164
Open Access Status Not yet assessed
Volume 95
Issue 1
Start page 164
End page 170
Total pages 7
Place of publication ROCKVILLE
Publisher AMER SOC PLANT PHYSIOLOGISTS
Language eng
Abstract A cDNA clone encoding a nonspecific lipid transfer protein from spinach (Spinacia oleracea) was isolated by probing a library with synthetic oligonucleotides based on the amino acid sequence of the protein. Determination of the DNA sequence indicated a 354-nucleotide open reading frame which encodes a 118-amino acid residue polypeptide. The first 26 amino acids of the open reading frame, which are not present in the mature protein, have all the characteristics of a signal sequence which is normally associated with the synthesis of membrane proteins or secreted proteins. In vitro transcription of the cDNA and translation in the presence of canine pancreatic microsomes or microsomes from cultured maize endosperm cells indicated that proteolytic processing of the preprotein to the mature form was associated with cotranslational insertion into the microsomal membranes. Because there is no known mechanism by which the polypeptide could be transferred from the microsomal membranes to the cytoplasm, the proposed role of this protein in catalyzing lipid transfer between intracellular membranes is in doubt. Although the lipid transfer protein is one of the most abundant proteins in leaf cells, the results of genomic Southern analysis were consistent with the presence of only one gene. Analysis of the level of mRNA by Northern blotting indicated that the transcript was several-fold more abundant than an actin transcript in leaf and petiole tissue, but was present in roots at less than 1% of the level in petioles.
Keyword Phospholipid-Transfer Protein
Amino-Acid-Sequence
Castor Bean Endosperms
Intracellular Exchange
Maize
Purification
Membranes
Translocation
Mitochondria
Chloroplasts
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: ResearcherID Downloads - Archived
 
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