| Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C. | |
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MedLine Citation:
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PMID: 1720555 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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B S Shorrosh; R A Dixon |
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Publication Detail:
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Type: Comparative Study; Journal Article |
Journal Detail:
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Title: Proceedings of the National Academy of Sciences of the United States of America Volume: 88 ISSN: 0027-8424 ISO Abbreviation: Proc. Natl. Acad. Sci. U.S.A. Publication Date: 1991 Dec |
Date Detail:
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Created Date: 1992-01-09 Completed Date: 1992-01-09 Revised Date: 2010-09-07 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 10941-5 Citation Subset: IM |
Affiliation:
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Plant Biology Division, Samuel Roberts Noble Foundation, Ardmore, OK 73402. |
| Data Bank Information | |
Bank Name/Acc. No.:
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GENBANK/M72335; M80723; M80724; M81661; M81662; M81664; M81665; M81666; M82973; S71210; S71212 |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Binding Sites Cells, Cultured Cloning, Molecular / methods DNA / genetics, isolation & purification Escherichia coli / genetics Gene Library Humans Isomerases / genetics* Macromolecular Substances Medicago sativa / enzymology, genetics* Membrane Proteins / genetics* Molecular Sequence Data Oligodeoxyribonucleotides Phosphatidylinositol Diacylglycerol-Lyase Phosphoinositide Phospholipase C Phosphoric Diester Hydrolases / genetics* Plant Proteins / genetics* Protein Disulfide-Isomerases RNA / genetics, isolation & purification Restriction Mapping Sequence Homology, Nucleic Acid Transcription, Genetic Vertebrates |
| Chemical | |
Reg. No./Substance:
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0/Macromolecular Substances; 0/Membrane Proteins; 0/Oligodeoxyribonucleotides; 0/Plant Proteins; 63231-63-0/RNA; 9007-49-2/DNA; EC 3.1.4.-/Phosphoric Diester Hydrolases; EC 3.1.4.11/Phosphoinositide Phospholipase C; EC 4.6.1.13/Phosphatidylinositol Diacylglycerol-Lyase; EC 5.-/Isomerases; EC 5.3.4.1/Protein Disulfide-Isomerases |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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