Identification and kinetics of accumulation of proteins induced by ethylene in bean abscission zones.
Identifieur interne : 000515 ( Main/Exploration ); précédent : 000514; suivant : 000516Identification and kinetics of accumulation of proteins induced by ethylene in bean abscission zones.
Auteurs : E. Del Campillo [États-Unis] ; L N LewisSource :
- Plant physiology [ 0032-0889 ] ; 1992.
Abstract
A two-dimensional gel electrophoresis system that combines a cationic polyacrylamide gel electrophoresis at pH near neutrality with sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to analyze the spectrum of basic polypeptides that accumulate in bean (Phaseolus vulgaris) abscission zones after treatment with ethylene. Results showed that, as abscission progressed, at least seven basic proteins accumulated in the abscission zone prior to the accumulation of 9.5 cellulase. Six of the seven proteins correspond to pathogenesis-related (PR) proteins. Among them, two isoforms of beta-1,3-glucanase and multiple isoforms of chitinase were identified. A 22 kilodalton polypeptide that accumulated to high levels was identified as a thaumatin-like protein by analysis of its N-terminal sequence (up to 20 amino acids) and its serological relationship with heterologous thaumatin antibodies. A 15 kilodalton polypeptide serologically related to PR P1 (p14) from tomato was identified as bean PR P1 (p14)-like protein. The kinetics of accumulation of glucanases, chitinases, thaumatin-like and PR P1 (p14)-like proteins during ethylene treatment were similar and they showed that PR proteins accumulated in abscission zones prior to the increase in 9.5 cellulase. Addition of indoleacetic acid, a potent inhibitor of abscission, reduced the accumulation of these proteins to a similar extent (60%). The synchronized accumulation of this set of PR proteins, early in the abscission process, may play a role in induced resistance to possible fungal attack after a plant part is shed. The seventh protein does not correspond to any previously characterized PR protein. This new 45 kilodalton polypeptide accumulated in abscission zones on exposure to ethylene concomitantly with the increase in 9.5 cellulase. Its N-terminal sequence (up to 15 amino acids) showed some homology with the amino terminal sequence of chitinase. Polyclonal antibodies against chitinase recognized the 45 kilodalton polypeptide, but polyclonal antibodies against the 45 kilodalton protein recognized chitinase weakly. When abscission was inhibited by addition of indoleacetic acid, the accumulation of the 45 kilodalton protein was strongly inhibited (80%). This result suggests that the 45 kilodalton polypeptide may play a more direct role in abscission.
DOI: 10.1104/pp.98.3.955
PubMed: 16668770
PubMed Central: PMC1080293
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Del Campillo</name><affiliation wicri:level="2"><nlm:affiliation>Department of Plant Biology, University of California at Berkeley, Berkeley, California 94720.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Plant Biology, University of California at Berkeley, Berkeley</wicri:cityArea></affiliation></author><author><name sortKey="Lewis, L N" sort="Lewis, L N" uniqKey="Lewis L" first="L N" last="Lewis">L N Lewis</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1992">1992</date><idno type="RBID">pubmed:16668770</idno><idno type="pmid">16668770</idno><idno type="pmc">PMC1080293</idno><idno type="doi">10.1104/pp.98.3.955</idno><idno type="wicri:Area/Main/Corpus">000513</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000513</idno><idno type="wicri:Area/Main/Curation">000513</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000513</idno><idno type="wicri:Area/Main/Exploration">000513</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Identification and kinetics of accumulation of proteins induced by ethylene in bean abscission zones.</title><author><name sortKey="Del Campillo, E" sort="Del Campillo, E" uniqKey="Del Campillo E" first="E" last="Del Campillo">E. Del Campillo</name><affiliation wicri:level="2"><nlm:affiliation>Department of Plant Biology, University of California at Berkeley, Berkeley, California 94720.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Plant Biology, University of California at Berkeley, Berkeley</wicri:cityArea></affiliation></author><author><name sortKey="Lewis, L N" sort="Lewis, L N" uniqKey="Lewis L" first="L N" last="Lewis">L N Lewis</name></author></analytic><series><title level="j">Plant physiology</title><idno type="ISSN">0032-0889</idno><imprint><date when="1992" type="published">1992</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A two-dimensional gel electrophoresis system that combines a cationic polyacrylamide gel electrophoresis at pH near neutrality with sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to analyze the spectrum of basic polypeptides that accumulate in bean (Phaseolus vulgaris) abscission zones after treatment with ethylene. Results showed that, as abscission progressed, at least seven basic proteins accumulated in the abscission zone prior to the accumulation of 9.5 cellulase. Six of the seven proteins correspond to pathogenesis-related (PR) proteins. Among them, two isoforms of beta-1,3-glucanase and multiple isoforms of chitinase were identified. A 22 kilodalton polypeptide that accumulated to high levels was identified as a thaumatin-like protein by analysis of its N-terminal sequence (up to 20 amino acids) and its serological relationship with heterologous thaumatin antibodies. A 15 kilodalton polypeptide serologically related to PR P1 (p14) from tomato was identified as bean PR P1 (p14)-like protein. The kinetics of accumulation of glucanases, chitinases, thaumatin-like and PR P1 (p14)-like proteins during ethylene treatment were similar and they showed that PR proteins accumulated in abscission zones prior to the increase in 9.5 cellulase. Addition of indoleacetic acid, a potent inhibitor of abscission, reduced the accumulation of these proteins to a similar extent (60%). The synchronized accumulation of this set of PR proteins, early in the abscission process, may play a role in induced resistance to possible fungal attack after a plant part is shed. The seventh protein does not correspond to any previously characterized PR protein. This new 45 kilodalton polypeptide accumulated in abscission zones on exposure to ethylene concomitantly with the increase in 9.5 cellulase. Its N-terminal sequence (up to 15 amino acids) showed some homology with the amino terminal sequence of chitinase. Polyclonal antibodies against chitinase recognized the 45 kilodalton polypeptide, but polyclonal antibodies against the 45 kilodalton protein recognized chitinase weakly. When abscission was inhibited by addition of indoleacetic acid, the accumulation of the 45 kilodalton protein was strongly inhibited (80%). This result suggests that the 45 kilodalton polypeptide may play a more direct role in abscission.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">16668770</PMID><DateCompleted><Year>2010</Year><Month>07</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>14</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>98</Volume><Issue>3</Issue><PubDate><Year>1992</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Identification and kinetics of accumulation of proteins induced by ethylene in bean abscission zones.</ArticleTitle><Pagination><MedlinePgn>955-61</MedlinePgn></Pagination><Abstract><AbstractText>A two-dimensional gel electrophoresis system that combines a cationic polyacrylamide gel electrophoresis at pH near neutrality with sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to analyze the spectrum of basic polypeptides that accumulate in bean (Phaseolus vulgaris) abscission zones after treatment with ethylene. Results showed that, as abscission progressed, at least seven basic proteins accumulated in the abscission zone prior to the accumulation of 9.5 cellulase. Six of the seven proteins correspond to pathogenesis-related (PR) proteins. Among them, two isoforms of beta-1,3-glucanase and multiple isoforms of chitinase were identified. A 22 kilodalton polypeptide that accumulated to high levels was identified as a thaumatin-like protein by analysis of its N-terminal sequence (up to 20 amino acids) and its serological relationship with heterologous thaumatin antibodies. A 15 kilodalton polypeptide serologically related to PR P1 (p14) from tomato was identified as bean PR P1 (p14)-like protein. The kinetics of accumulation of glucanases, chitinases, thaumatin-like and PR P1 (p14)-like proteins during ethylene treatment were similar and they showed that PR proteins accumulated in abscission zones prior to the increase in 9.5 cellulase. Addition of indoleacetic acid, a potent inhibitor of abscission, reduced the accumulation of these proteins to a similar extent (60%). The synchronized accumulation of this set of PR proteins, early in the abscission process, may play a role in induced resistance to possible fungal attack after a plant part is shed. The seventh protein does not correspond to any previously characterized PR protein. This new 45 kilodalton polypeptide accumulated in abscission zones on exposure to ethylene concomitantly with the increase in 9.5 cellulase. Its N-terminal sequence (up to 15 amino acids) showed some homology with the amino terminal sequence of chitinase. Polyclonal antibodies against chitinase recognized the 45 kilodalton polypeptide, but polyclonal antibodies against the 45 kilodalton protein recognized chitinase weakly. When abscission was inhibited by addition of indoleacetic acid, the accumulation of the 45 kilodalton protein was strongly inhibited (80%). This result suggests that the 45 kilodalton polypeptide may play a more direct role in abscission.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Del Campillo</LastName><ForeName>E</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Plant Biology, University of California at Berkeley, Berkeley, California 94720.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lewis</LastName><ForeName>L N</ForeName><Initials>LN</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1992</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1992</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1992</Year><Month>3</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16668770</ArticleId><ArticleId IdType="pmc">PMC1080293</ArticleId><ArticleId IdType="doi">10.1104/pp.98.3.955</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Nature. 1970 Aug 15;227(5259):680-5</Citation><ArticleIdList><ArticleId IdType="pubmed">5432063</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 1990 Mar;2(3):245-254</Citation><ArticleIdList><ArticleId IdType="pubmed">12354957</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1970 Apr;45(4):395-400</Citation><ArticleIdList><ArticleId IdType="pubmed">5427109</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1984 Feb;74(2):442-4</Citation><ArticleIdList><ArticleId IdType="pubmed">16663439</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Cell. 1989 Jun;1(6):599-607</Citation><ArticleIdList><ArticleId IdType="pubmed">2535512</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1991 Jul;96(3):943-51</Citation><ArticleIdList><ArticleId IdType="pubmed">16668279</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Mol Biol. 1990 Mar;14(3):357-68</Citation><ArticleIdList><ArticleId IdType="pubmed">1966383</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1968 Sep;43(9 Pt B):1577-86</Citation><ArticleIdList><ArticleId IdType="pubmed">16657020</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 1955 Dec;217(2):959-66</Citation><ArticleIdList><ArticleId IdType="pubmed">13271455</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 1986 Sep;83(18):6820-4</Citation><ArticleIdList><ArticleId IdType="pubmed">2428042</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1981 Nov 15;118(1):194-6</Citation><ArticleIdList><ArticleId IdType="pubmed">6278979</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Physiol. 1988 Dec;88(4):1257-62</Citation><ArticleIdList><ArticleId IdType="pubmed">16666452</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 1986 May 29-Jun 4;321(6069):531-2</Citation><ArticleIdList><ArticleId IdType="pubmed">3713832</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Biochem. 1973 Dec;56(2):502-14</Citation><ArticleIdList><ArticleId IdType="pubmed">4128882</ArticleId></ArticleIdList></Reference><Reference><Citation>Mol Gen Genet. 1989 Jan;215(2):200-8</Citation><ArticleIdList><ArticleId IdType="pubmed">2710099</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant Mol Biol. 1991 Jan;16(1):81-94</Citation><ArticleIdList><ArticleId IdType="pubmed">1909591</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Californie</li></region></list><tree><noCountry><name sortKey="Lewis, L N" sort="Lewis, L N" uniqKey="Lewis L" first="L N" last="Lewis">L N Lewis</name></noCountry><country name="États-Unis"><region name="Californie"><name sortKey="Del Campillo, E" sort="Del Campillo, E" uniqKey="Del Campillo E" first="E" last="Del Campillo">E. 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