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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
51
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pubmed:dateCreated |
2004-12-13
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pubmed:abstractText |
This is the first report describing the cloning and characterization of sterol carrier protein-2 (SCP-2) from plants. Arabidopsis thaliana SCP-2 (AtSCP-2) consists of 123 amino acids with a molecular mass of 13.6 kDa. AtSCP-2 shows 35% identity and 56% similarity to the human SCP-2-like domain present in the human D-bifunctional protein (DBP) and 30% identity and 54% similarity to the human SCP-2 encoded by SCP-X. The presented structural models of apo-AtSCP-2 and the ligand-bound conformation of AtSCP-2 reveal remarkable similarity with two of the structurally known SCP-2s, the SCP-2-like domain of human DBP and the rabbit SCP-2, correspondingly. The AtSCP-2 models in both forms have a similar hydrophobic ligand-binding tunnel, which is extremely suitable for lipid binding. AtSCP-2 showed in vitro transfer activity of BODIPY-phosphatidylcholine (BODIPY-PC) from donor membranes to acceptor membranes. The transfer of BODIPY-PC was almost completely inhibited after addition of 1-palmitoyl 2-oleoyl phosphatidylcholine or ergosterol. Dimyristoyl phosphatidic acid, stigmasterol, steryl glucoside, and cholesterol showed a moderate to marginal ability to lower the BODIPY-PC transfer rate, and the single chain palmitic acid and stearoyl-coenzyme A did not affect transfer at all. Expression analysis showed that AtSCP-2 mRNA is accumulating in most plant tissues. Plasmids carrying fusion genes between green fluorescent protein and AtSCP-2 were transformed with particle bombardment to onion epidermal cells. The results from analyzing the transformants indicate that AtSCP-2 is localized to peroxisomes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4,4-difluoro-4-bora-3a,4a-diaza-s-in...,
http://linkedlifedata.com/resource/pubmed/chemical/Agar,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Boron Compounds,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/Ergosterol,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosides,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycerophospholipids,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Palmitic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sterols,
http://linkedlifedata.com/resource/pubmed/chemical/Stigmasterol,
http://linkedlifedata.com/resource/pubmed/chemical/dimyristoylphosphatidic acid,
http://linkedlifedata.com/resource/pubmed/chemical/lipid transfer proteins, plant,
http://linkedlifedata.com/resource/pubmed/chemical/sterol carrier proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
279
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
53544-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15456765-Humans,
pubmed-meshheading:15456765-Animals,
pubmed-meshheading:15456765-Lipids,
pubmed-meshheading:15456765-Cholesterol,
pubmed-meshheading:15456765-Glucosides,
pubmed-meshheading:15456765-Agar,
pubmed-meshheading:15456765-Sterols,
pubmed-meshheading:15456765-Fluorescent Dyes,
pubmed-meshheading:15456765-Boron Compounds,
pubmed-meshheading:15456765-Phosphatidylcholines,
pubmed-meshheading:15456765-Ergosterol,
pubmed-meshheading:15456765-Palmitic Acid,
pubmed-meshheading:15456765-Onions,
pubmed-meshheading:15456765-Rabbits,
pubmed-meshheading:15456765-Escherichia coli,
pubmed-meshheading:15456765-RNA,
pubmed-meshheading:15456765-Plant Proteins,
pubmed-meshheading:15456765-Models, Molecular,
pubmed-meshheading:15456765-Protein Conformation,
pubmed-meshheading:15456765-Time Factors,
pubmed-meshheading:15456765-Amino Acid Sequence,
pubmed-meshheading:15456765-Models, Chemical,
pubmed-meshheading:15456765-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:15456765-Molecular Sequence Data,
pubmed-meshheading:15456765-Binding, Competitive,
pubmed-meshheading:15456765-Phylogeny,
pubmed-meshheading:15456765-Carrier Proteins,
pubmed-meshheading:15456765-Protein Structure, Secondary,
pubmed-meshheading:15456765-Protein Structure, Tertiary,
pubmed-meshheading:15456765-Cloning, Molecular,
pubmed-meshheading:15456765-Sequence Homology, Amino Acid,
pubmed-meshheading:15456765-Plasmids,
pubmed-meshheading:15456765-Stigmasterol,
pubmed-meshheading:15456765-Arabidopsis,
pubmed-meshheading:15456765-Glutathione Transferase,
pubmed-meshheading:15456765-Recombinant Proteins,
pubmed-meshheading:15456765-Peroxisomes,
pubmed-meshheading:15456765-Antigens, Plant,
pubmed-meshheading:15456765-Glycerophospholipids,
pubmed-meshheading:15456765-Computational Biology,
pubmed-meshheading:15456765-Green Fluorescent Proteins,
pubmed-meshheading:15456765-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:15456765-Fluorescence Resonance Energy Transfer
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