Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis
Identifieur interne : 000647 ( Pmc/Curation ); précédent : 000646; suivant : 000648Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis
Auteurs : Renu Srivastava ; Jian-Xiang Liu ; Stephen H. HowellSource :
- The Plant Journal [ 0960-7412 ] ; 2008.
Abstract
Phytosulfokines (PSKs) are secreted, sulfated peptide hormones derived from larger prepropeptide precursors. Proteolytic processing of one of the precursors, AtPSK4, was demonstrated by cleavage of a preproAtPSK4–myc transgene product to AtPSK4–myc. Cleavage of proAtPSK4 was induced by placing root explants in tissue culture. The processing of proAtPSK4 was dependent on AtSBT1.1, a subtilisin-like serine protease, encoded by one of 56 subtilase genes in Arabidopsis. The gene encoding AtSBT1.1 was up-regulated following the transfer of root explants to tissue culture, suggesting that activation of the proteolytic machinery that cleaves proAtPSK4 is dependent on AtSBT1.1 expression. We also demonstrated that a fluorogenic peptide representing the putative subtilase recognition site in proAtPSK4 is cleaved
Url:
DOI: 10.1111/j.1365-313X.2008.03598.x
PubMed: 18643977
PubMed Central: 2667306
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Plant J</journal-id><journal-id journal-id-type="publisher-id">tpj</journal-id><journal-title>The Plant Journal </journal-title><issn pub-type="ppub">0960-7412</issn><issn pub-type="epub">1365-313X</issn><publisher><publisher-name>Blackwell Publishing Ltd</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">18643977</article-id><article-id pub-id-type="pmc">2667306</article-id><article-id pub-id-type="doi">10.1111/j.1365-313X.2008.03598.x</article-id><article-categories><subj-group subj-group-type="heading"><subject>Original Articles</subject></subj-group></article-categories><title-group><article-title>Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Srivastava</surname><given-names>Renu</given-names></name></contrib><contrib contrib-type="author"><name><surname>Liu</surname><given-names>Jian-Xiang</given-names></name></contrib><contrib contrib-type="author"><name><surname>Howell</surname><given-names>Stephen H</given-names></name><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff><institution>Plant Sciences Institute, Iowa State University</institution><addr-line>Ames, IA 50011, USA</addr-line></aff></contrib-group><author-notes><corresp id="cor1">* For correspondence (fax +1 515 294 5256; e-mail <email>shh@iastate.edu</email>).</corresp></author-notes><pub-date pub-type="ppub"><month>10</month><year>2008</year></pub-date><pub-date pub-type="epub"><day>01</day><month>8</month><year>2008</year></pub-date><volume>56</volume><issue>2</issue><fpage>219</fpage><lpage>227</lpage><history><date date-type="received"><day>23</day><month>1</month><year>2008</year></date><date date-type="rev-recd"><day>01</day><month>5</month><year>2008</year></date><date date-type="accepted"><day>12</day><month>5</month><year>2008</year></date></history><copyright-statement>© 2008 The Authors. Journal compilation © 2008 Blackwell Publishing Ltd</copyright-statement><copyright-year>2008</copyright-year><license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/2.5/"><p>Reuse of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.</p></license><abstract><p>Phytosulfokines (PSKs) are secreted, sulfated peptide hormones derived from larger prepropeptide precursors. Proteolytic processing of one of the precursors, AtPSK4, was demonstrated by cleavage of a preproAtPSK4–myc transgene product to AtPSK4–myc. Cleavage of proAtPSK4 was induced by placing root explants in tissue culture. The processing of proAtPSK4 was dependent on AtSBT1.1, a subtilisin-like serine protease, encoded by one of 56 subtilase genes in Arabidopsis. The gene encoding AtSBT1.1 was up-regulated following the transfer of root explants to tissue culture, suggesting that activation of the proteolytic machinery that cleaves proAtPSK4 is dependent on AtSBT1.1 expression. We also demonstrated that a fluorogenic peptide representing the putative subtilase recognition site in proAtPSK4 is cleaved <italic>in vitro</italic> by affinity-purified AtSBT1.1. An alanine scan through the recognition site peptide indicated that AtSBT1.1 is fairly specific for the AtPSK4 precursor. Thus, this peptide growth factor, which promotes callus formation in culture, is proteolytically cleaved from its precursor by a specific plant subtilase encoded by a gene that is up-regulated during the process of transfering root explants to tissue culture.</p></abstract><kwd-group><kwd>Arabidopsis</kwd><kwd>phytosulfokine</kwd><kwd>subtilase</kwd><kwd>peptide hormone</kwd><kwd>tissue culture</kwd><kwd>fluorogenic peptide</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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