NDLI: Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C.

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Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C.

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Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Shorrosh, B. S. Dixon, R. A.
Description	Author Affiliation: Shorrosh BS ( Plant Biology Division, Samuel Roberts Noble Foundation, Ardmore, OK 73402.);
Abstract	cDNA clones containing sequence similarity to the multifunctional vertebrate protein disulfide-isomerase (PDI, EC 5.3.4.1) were isolated from an alfalfa (Medicago sativa L.) cDNA library by screening with a cDNA sequence encoding human PDI. The polypeptide encoded by a clone designated B2 consisted of 512 amino acids and was characterized by a 24-amino acid hydrophobic leader sequence, two regions with absolute identity to the vertebrate PDI active site (Ala-Pro-Trp-Cys-Gly-His-Cys-Lys), and a C-terminal endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu). The overall identity of the B2 sequence to that of human PDI was 35% at the amino acid level (79% when conservative substitutions were included) and 39% at the nucleotide level; this included homology between B2 and the region of human PDI believed to be involved in binding estrogens. The deduced amino acid sequence of B2 was also 35% identical to that of a rat form I phosphatidylinositol-specific phospholipase C. Lysates from Escherichia coli cells harboring an expression plasmid bearing the B2 sequence contained significantly elevated levels of PDI activity. Southern analysis indicated the presence of a small PDI-related gene family in alfalfa, of which B2 appeared to correspond to a single gene. An approximately 2-kilobase B2 transcript was expressed in all alfalfa organs tested. In alfalfa cell suspension cultures, B2 transcripts were strongly induced by tunicamycin but not by exposure to fungal elicitor.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	88
Language	English
Publisher	National Academy of Sciences
Publisher Date	1991-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Isomerases Genetics Medicago Sativa Membrane Proteins Phosphoric Diester Hydrolases Plant Proteins Amino Acid Sequence Animals Binding Sites Cells, Cultured Cloning, Molecular DNA Isolation & Purification Escherichia Coli Gene Library Macromolecular Substances Enzymology Molecular Sequence Data Oligodeoxyribonucleotides Phosphatidylinositol Diacylglycerol-Lyase Phosphoinositide Phospholipase C Protein Disulfide-Isomerases RNA Restriction Mapping Sequence Homology, Nucleic Acid Transcription, Genetic Vertebrates Comparative Study Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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