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Article: Differential accumulation of transcripts for four tomato 1- aminocyclopropane-1-carboxylate synthase homologs under various conditions

TitleDifferential accumulation of transcripts for four tomato 1- aminocyclopropane-1-carboxylate synthase homologs under various conditions
Authors
Issue Date1992
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings Of The National Academy Of Sciences Of The United States Of America, 1992, v. 89 n. 6, p. 2475-2479 How to Cite?
AbstractDegenerate oligonucleotide primers corresponding to conserved regions flanking the active-site domain of 1-aminocyclopropane-1-carboxylate (ACC) synthase (EC 4.4.1.14) were used for the polymerase chain reaction (PCR) to amplify DNA fragments from mRNA isolated from tomato fruit and tomato suspension cell culture. Antibodies raised against two conserved peptide sequences (TNPSNPLGTT and SLSKDLGLPGFRVG) were used to screen for positive colonies, after the PCR products were cloned into a Bluescript plasmid and expressed in Escherichia coli. Four distinct cDNA fragments encoding ACC synthase homologs were isolated. While pBTAS1 and pBTAS4 were obtained from fruit mRNA, cell culture mRNA yielded three sequences, pBTAS1, pBTAS2, and pBTAS3. Sequencing of these gene fragments revealed that pBTAS1 and pBTAS4 were identical to those full-length sequences previously reported by Van Der Straeten et al. [Van Der Straeten, D., Van Wiemeersch, L., Goodman, H. and Van Montague, M. (1990) Proc. Natl. Acad. Sci. USA 87, 4859-4863] and Olson et al. [Olson, D. C., White, J. A., Edelman, J., Harkin, R. N. and Kende, H. (1991) Proc. Natl. Acad. Sci. USA 88, 5340-5344] from tomato fruit, whereas pBTAS2 and pBTAS3 represent new sequences. Ribonuclease protection assays were used to examine the expression of these transcripts under three different conditions of enhanced ethylene production-namely, during fruit ripening, in response to mechanical wounding in fruit tissue, and auxin stimulation in vegetative tissue. Transcripts of pBTAS1 accumulated massively during ripening and wounding but only slightly in response to auxin treatment. Although pBTAS4 was associated with fruit ripening, it was unresponsive to auxin treatment in vegetative tissue. In contrast, the expression of pBTAS2 and pBTAS3 was greatly promoted in auxin-treated vegetative tissue but was absent from fruit tissue. While the expression of pBTAS2 was moderately dependent on wounding, pBTAS3 was unresponsive to wounding. These data support the view that ACC synthase is encoded by a multigene family and that the members are differentially expressed in response to developmental, environmental, and hormonal factors.
Persistent Identifierhttp://hdl.handle.net/10722/178525
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYip, WKen_US
dc.contributor.authorMoore, Ten_US
dc.contributor.authorShang Fa Yangen_US
dc.date.accessioned2012-12-19T09:48:13Z-
dc.date.available2012-12-19T09:48:13Z-
dc.date.issued1992en_US
dc.identifier.citationProceedings Of The National Academy Of Sciences Of The United States Of America, 1992, v. 89 n. 6, p. 2475-2479en_US
dc.identifier.issn0027-8424en_US
dc.identifier.urihttp://hdl.handle.net/10722/178525-
dc.description.abstractDegenerate oligonucleotide primers corresponding to conserved regions flanking the active-site domain of 1-aminocyclopropane-1-carboxylate (ACC) synthase (EC 4.4.1.14) were used for the polymerase chain reaction (PCR) to amplify DNA fragments from mRNA isolated from tomato fruit and tomato suspension cell culture. Antibodies raised against two conserved peptide sequences (TNPSNPLGTT and SLSKDLGLPGFRVG) were used to screen for positive colonies, after the PCR products were cloned into a Bluescript plasmid and expressed in Escherichia coli. Four distinct cDNA fragments encoding ACC synthase homologs were isolated. While pBTAS1 and pBTAS4 were obtained from fruit mRNA, cell culture mRNA yielded three sequences, pBTAS1, pBTAS2, and pBTAS3. Sequencing of these gene fragments revealed that pBTAS1 and pBTAS4 were identical to those full-length sequences previously reported by Van Der Straeten et al. [Van Der Straeten, D., Van Wiemeersch, L., Goodman, H. and Van Montague, M. (1990) Proc. Natl. Acad. Sci. USA 87, 4859-4863] and Olson et al. [Olson, D. C., White, J. A., Edelman, J., Harkin, R. N. and Kende, H. (1991) Proc. Natl. Acad. Sci. USA 88, 5340-5344] from tomato fruit, whereas pBTAS2 and pBTAS3 represent new sequences. Ribonuclease protection assays were used to examine the expression of these transcripts under three different conditions of enhanced ethylene production-namely, during fruit ripening, in response to mechanical wounding in fruit tissue, and auxin stimulation in vegetative tissue. Transcripts of pBTAS1 accumulated massively during ripening and wounding but only slightly in response to auxin treatment. Although pBTAS4 was associated with fruit ripening, it was unresponsive to auxin treatment in vegetative tissue. In contrast, the expression of pBTAS2 and pBTAS3 was greatly promoted in auxin-treated vegetative tissue but was absent from fruit tissue. While the expression of pBTAS2 was moderately dependent on wounding, pBTAS3 was unresponsive to wounding. These data support the view that ACC synthase is encoded by a multigene family and that the members are differentially expressed in response to developmental, environmental, and hormonal factors.en_US
dc.languageengen_US
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_US
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAntibodiesen_US
dc.subject.meshBase Sequenceen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshDna - Genetics - Isolation & Purificationen_US
dc.subject.meshLyases - Analysis - Geneticsen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMultigene Familyen_US
dc.subject.meshOligodeoxyribonucleotidesen_US
dc.subject.meshPeptides - Chemical Synthesis - Immunologyen_US
dc.subject.meshPlants - Enzymology - Geneticsen_US
dc.subject.meshPlasmidsen_US
dc.subject.meshPolymerase Chain Reactionen_US
dc.subject.meshRna, Messenger - Genetics - Isolation & Purificationen_US
dc.subject.meshRestriction Mappingen_US
dc.subject.meshSequence Homology, Nucleic Aciden_US
dc.subject.meshTranscription, Geneticen_US
dc.titleDifferential accumulation of transcripts for four tomato 1- aminocyclopropane-1-carboxylate synthase homologs under various conditionsen_US
dc.typeArticleen_US
dc.identifier.emailYip, WK: wkyip@hkucc.hku.hken_US
dc.identifier.authorityYip, WK=rp00833en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1073/pnas.89.6.2475-
dc.identifier.pmid1549612-
dc.identifier.scopuseid_2-s2.0-0026520787en_US
dc.identifier.volume89en_US
dc.identifier.issue6en_US
dc.identifier.spage2475en_US
dc.identifier.epage2479en_US
dc.identifier.isiWOS:A1992HJ05300099-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridYip, WK=7102784428en_US
dc.identifier.scopusauthoridMoore, T=7403336644en_US
dc.identifier.scopusauthoridShang Fa Yang=7409690533en_US

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