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Characterization of the closely related Arabidopsis thaliana ß-ketoacyl-CoA synthases KCS3, KCS12 and KCS19.
Zhang, Zhonghang; Gozdzik, Jedrzej; Jetter, Reinhard.
Afiliação
  • Zhang Z; Department of Botany, University of British Columbia, Vancouver, British Columbia, V6T 1Z4, Canada.
  • Gozdzik J; Department of Chemistry, University of British Columbia, Vancouver, British Columbia, V6T 1Z1, Canada.
  • Jetter R; Department of Botany, University of British Columbia, Vancouver, British Columbia, V6T 1Z4, Canada.
Plant J ; 119(1): 490-507, 2024 Jul.
Article em En | MEDLINE | ID: mdl-38666591
ABSTRACT
The cuticle, consisting of cuticular wax and cutin, is a lipid membrane that seals the plant surface against environmental stress. ß-Ketoacyl-CoA synthases (KCSs) are condensing enzymes catalyzing crucial reactions elongating hydrocarbon chains into precursors for various cuticular wax components. Although many KCS genes were well characterized in various species, the functions of the closely related Arabidopsis KCS3, KCS12, KCS19 enzymes remained unclear. Here, we found KCS3 preferentially expressed in growing organs, especially in guard cells. kcs3 mutants and kcs3kcs12 double mutants displayed sepal fusion phenotypes, suggesting defects in cuticle formation. The mutants had decreased amounts of wax components with relatively short hydrocarbon chains in the developing organs but increased levels of wax compounds in mature organs. In contrast, kcs19 mutants showed seed fusion phenotypes and altered chain length distributions in seed suberin. Taken together, our results show that KCS12 and KCS3 share redundant functions in flower development, while KCS19 is involved in seed coat formation. All three condensing enzymes are involved in the elongation of C>18 hydrocarbon chains in young, actively expanding tissues.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: Plant J Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Arabidopsis / Proteínas de Arabidopsis Idioma: En Revista: Plant J Ano de publicação: 2024 Tipo de documento: Article