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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
42
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pubmed:dateCreated |
2005-10-17
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pubmed:abstractText |
The Arabidopsis BRS1 gene encodes a serine carboxypeptidase II-like protein. Its biological role in the brassinosteroid signaling pathway was first established by its capability to specifically suppress a weak brassinosteroid insensitive 1 (bri1) allele, bri1-5, when overexpressed. To gain additional insights into the molecular mechanisms of BRS1 function, the subcellular localization and the biochemical characteristics of BRS1 were determined by using transgenic plants harboring a 35S-BRS1-GFP construct and fusion proteins purified from 35S-BRS1-FLAG transgenic plants. The BRS1-GFP protein was mainly secreted and accumulated in the extracellular space. Immunological data suggest that BRS1 is proteolytically processed by an unknown endoproteinase in planta. Affinity-purified BRS1-FLAG from transgenic plants show strong hydrolytic activity with a broad P1 substrate preference including basic and hydrophobic groups on either side of the scissile bond. The hydrolytic activity of BRS1 can be strongly inhibited by a serine protease inhibitor, phenylmethylsulfonyl fluoride. The pH and temperature optima for the hydrolytic activity of BRS1 are pH 5.5 and 50 degrees C, respectively. These data demonstrate that BRS1 is a secreted and active serine carboxypeptidase, consistent with the hypothesis suggested by our previous genetic evidence that BRS1 may process a protein involved in an early event in the BRI1 signaling pathway.
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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/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/BRS1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Carboxypeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phenylmethylsulfonyl Fluoride,
http://linkedlifedata.com/resource/pubmed/chemical/serine carboxypeptidase
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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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 |
21
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pubmed:volume |
280
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35554-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16123046-Alleles,
pubmed-meshheading:16123046-Amino Acid Sequence,
pubmed-meshheading:16123046-Arabidopsis,
pubmed-meshheading:16123046-Arabidopsis Proteins,
pubmed-meshheading:16123046-Blotting, Western,
pubmed-meshheading:16123046-Carboxypeptidases,
pubmed-meshheading:16123046-Chromatography, Affinity,
pubmed-meshheading:16123046-DNA, Complementary,
pubmed-meshheading:16123046-Enzyme Inhibitors,
pubmed-meshheading:16123046-Gene Expression Regulation, Plant,
pubmed-meshheading:16123046-Glycosylation,
pubmed-meshheading:16123046-Green Fluorescent Proteins,
pubmed-meshheading:16123046-Homozygote,
pubmed-meshheading:16123046-Hydrogen-Ion Concentration,
pubmed-meshheading:16123046-Hydrolysis,
pubmed-meshheading:16123046-Mass Spectrometry,
pubmed-meshheading:16123046-Microscopy, Confocal,
pubmed-meshheading:16123046-Molecular Sequence Data,
pubmed-meshheading:16123046-Mutation,
pubmed-meshheading:16123046-Peptides,
pubmed-meshheading:16123046-Phenotype,
pubmed-meshheading:16123046-Phenylmethylsulfonyl Fluoride,
pubmed-meshheading:16123046-Plants, Genetically Modified,
pubmed-meshheading:16123046-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:16123046-Signal Transduction,
pubmed-meshheading:16123046-Substrate Specificity,
pubmed-meshheading:16123046-Temperature,
pubmed-meshheading:16123046-Time Factors,
pubmed-meshheading:16123046-Transgenes
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pubmed:year |
2005
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pubmed:articleTitle |
Arabidopsis BRS1 is a secreted and active serine carboxypeptidase.
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pubmed:affiliation |
Department of Botany and Microbiology, University of Oklahoma, Norman, Oklahoma 73019, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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