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OAS-TL enzyme isoforms are localised in the cytoplasm, the plastids and mitochondria but the contribution of individual OAS-TL isoforms to plant sulphur metabolism has not yet been fully clarified.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>The seedling lethal phenotype of the <jats:italic>Arabidopsis onset of leaf death3-1<\/jats:italic> (<jats:italic>old3-1<\/jats:italic>) mutant is due to a point mutation in the <jats:italic>OAS-A1<\/jats:italic> gene, encoding the cytosolic OAS-TL. The mutation causes a single amino acid substitution from Gly<jats:sup>162<\/jats:sup> to Glu<jats:sup>162<\/jats:sup>, abolishing old3-1 OAS-TL activity <jats:italic>in vitro<\/jats:italic>. The <jats:italic>old3-1<\/jats:italic> mutation segregates as a monogenic semi-dominant trait when backcrossed to its wild type accession Landsberg <jats:italic>erecta<\/jats:italic> (L<jats:italic>er<\/jats:italic>-0) and the Di-2 accession. Consistent with its semi-dominant behaviour, wild type L<jats:italic>er<\/jats:italic>-0 plants transformed with the mutated <jats:italic>old3-1<\/jats:italic> gene, displayed the early leaf death phenotype. However, the <jats:italic>old3-1<\/jats:italic> mutation segregates in an 11:4:1 (wild type: semi-dominant: mutant) ratio when backcrossed to the Colombia-0 and Wassilewskija accessions. Thus, the early leaf death phenotype depends on two semi-dominant loci. The second locus that determines the <jats:italic>old3-1<\/jats:italic> early leaf death phenotype is referred to as <jats:italic>odd-ler<\/jats:italic> (for <jats:italic>\n                <jats:underline>o<\/jats:underline>\n              <\/jats:italic>\n              <jats:italic>l<\/jats:italic>\n              <jats:italic>\n                <jats:underline>d<\/jats:underline>\n              <\/jats:italic>\n              <jats:italic>3<\/jats:italic>\n              <jats:underline>d<\/jats:underline>eterminant in the L<jats:italic>er<\/jats:italic> accession) and is located on chromosome 3. The early leaf death phenotype is temperature dependent and is associated with increased expression of defence-response and oxidative-stress marker genes. Independent of the presence of the <jats:italic>odd-ler<\/jats:italic> gene, <jats:italic>OAS-A1<\/jats:italic> is involved in maintaining sulphur and thiol levels and is required for resistance against cadmium stress.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusions<\/jats:title>\n            <jats:p>The cytosolic OAS-TL is involved in maintaining organic sulphur levels. The <jats:italic>old3-1<\/jats:italic> mutation causes genome-dependent and independent phenotypes and uncovers a novel function for the mutated OAS-TL in cell death regulation.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2229-10-80","type":"journal-article","created":{"date-parts":[[2010,4,29]],"date-time":"2010-04-29T18:15:30Z","timestamp":1272564930000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":30,"title":["A mutation in the cytosolic O-acetylserine (thiol) lyase induces a genome-dependent early leaf death phenotype in Arabidopsis"],"prefix":"10.1186","volume":"10","author":[{"given":"Reza","family":"Shirzadian-Khorramabad","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hai-Chun","family":"Jing","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gerja E","family":"Everts","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jos HM","family":"Schippers","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacques","family":"Hille","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul P","family":"Dijkwel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2010,4,29]]},"reference":[{"issue":"2","key":"574_CR1","doi-asserted-by":"publisher","first-page":"625","DOI":"10.1105\/tpc.106.043125","volume":"19","author":"M Wirtz","year":"2007","unstructured":"Wirtz M, Hell R: Dominant-negative modification reveals the regulatory function of the multimeric cysteine synthase protein complex in transgenic tobacco. 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