Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-2-22
pubmed:databankReference
pubmed:abstractText
We used 5-azido-[7-3H]indole-3-acetic acid (5-azido-[7-3H]IAA), a photoaffinity analogue of the plant hormone indole-3-acetic acid (IAA), to search for auxin-binding proteins in Arabidopsis thaliana membranes. We identified an auxin-binding protein with a molecular mass of 24 kDa (Atpm24) in microsomes as well as in plasma membrane vesicles. Atpm24 was solubilized by 1% Triton X-100 and partially purified. A cDNA clone (Atpm24.1) corresponding to Atpm24 was isolated. The amino acid sequence predicted from the Atpm24.1 cDNA contains 212 amino acid residues with a relative molecular mass of 24,128 Da. Data base searches revealed that the predicted protein has homology to glutathione S-transferases (GSTs; EC 2.5.1.18). When Atpm24.1 was expressed in Escherichia coli, we found a high level of GST activity in the bacterial extracts. We have analyzed the substrate specificity of this protein and found that cumene hydroperoxide and trans-stilbene oxide but not trans-cinnamic acid or IAA-CoA were substrates. A role for this GST in physiological processes of plants is discussed.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-11537412, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-11537490, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-11607251, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-1522586, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-16594060, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-1729717, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-1799693, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-1850406, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-2065650, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-2199796, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-3069329, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-3277162, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-3372534, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-6301011, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-666896, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-6884349, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-6989596, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-7173206, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-8108497, http://linkedlifedata.com/resource/pubmed/commentcorrection/8290582-8329687
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
689-93
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed-meshheading:8290582-Affinity Labels, pubmed-meshheading:8290582-Amino Acid Sequence, pubmed-meshheading:8290582-Arabidopsis, pubmed-meshheading:8290582-Azides, pubmed-meshheading:8290582-Base Sequence, pubmed-meshheading:8290582-Cell Membrane, pubmed-meshheading:8290582-Cloning, Molecular, pubmed-meshheading:8290582-DNA Primers, pubmed-meshheading:8290582-Escherichia coli, pubmed-meshheading:8290582-Glutathione Transferase, pubmed-meshheading:8290582-Indoleacetic Acids, pubmed-meshheading:8290582-Molecular Sequence Data, pubmed-meshheading:8290582-Molecular Weight, pubmed-meshheading:8290582-Plant Growth Regulators, pubmed-meshheading:8290582-Plant Proteins, pubmed-meshheading:8290582-Receptors, Cell Surface, pubmed-meshheading:8290582-Sequence Homology, Amino Acid, pubmed-meshheading:8290582-Substrate Specificity
pubmed:year
1994
pubmed:articleTitle
Photoaffinity labeling of Arabidopsis thaliana plasma membrane vesicles by 5-azido-[7-3H]indole-3-acetic acid: identification of a glutathione S-transferase.
pubmed:affiliation
Max-Planck-Institut für Züchtungsforschung, Cologne, Federal Republic of Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't