| pubmed-article:16123046 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16123046 | lifeskim:mentions | umls-concept:C0162741 | lld:lifeskim |
| pubmed-article:16123046 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:16123046 | lifeskim:mentions | umls-concept:C0205177 | lld:lifeskim |
| pubmed-article:16123046 | lifeskim:mentions | umls-concept:C0074367 | lld:lifeskim |
| pubmed-article:16123046 | pubmed:issue | 42 | lld:pubmed |
| pubmed-article:16123046 | pubmed:dateCreated | 2005-10-17 | lld:pubmed |
| pubmed-article:16123046 | 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. | lld:pubmed |
| pubmed-article:16123046 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:16123046 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16123046 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16123046 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16123046 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:16123046 | pubmed:author | pubmed-author:OsL OLO | lld:pubmed |
| pubmed-article:16123046 | pubmed:author | pubmed-author:ZhouAifenA | lld:pubmed |
| pubmed-article:16123046 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16123046 | pubmed:day | 21 | lld:pubmed |
| pubmed-article:16123046 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:16123046 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16123046 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16123046 | pubmed:pagination | 35554-61 | lld:pubmed |
| pubmed-article:16123046 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16123046 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16123046 | pubmed:articleTitle | Arabidopsis BRS1 is a secreted and active serine carboxypeptidase. | lld:pubmed |
| pubmed-article:16123046 | pubmed:affiliation | Department of Botany and Microbiology, University of Oklahoma, Norman, Oklahoma 73019, USA. | lld:pubmed |
| pubmed-article:16123046 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16123046 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16123046 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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