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Type: Artigo
Title: Sugarcane Serine Peptidase Inhibitors, Serine Peptidases, And Clp Protease System Subunits Associated With Sugarcane Borer (diatraea Saccharalis) Herbivory And Wounding
Author: Medeiros
Ane H.; Mingossi
Fabiana B.; Dias
Renata O.; Franco
Flavia P.; Vicentini
Renato; Mello
Marcia O.; Moura
Daniel S.; Silva-Filho
Marcio C.
Abstract: Sugarcane's (Saccharum spp.) response to Diatraea saccharalis (F.) (Lepidoptera: (Crambidae) herbivory was investigated using a macroarray spotted with 248 sugarcane Expressed Sequence Tags (ESTs) encoding serine peptidase inhibitors, serine peptidases. and Clp protease system subunits. Our results showed that after nine hours of herbivory, 13 sugarcane genes were upregulated and nine were downregulated. Among the upregulated genes, nine were similar to serine peptidase inhibitors and four were similar to Bowman-Birk Inhibitors (BBIs). Phylogenetic analysis revealed that these sequences belong to a phylogenetic group of sugarcane BBIs that are potentially involved in plant defense against insect predation. The remaining four upregulated genes included serine peptidases and one homolog to the Arabidopsis AAA+ chaperone subunit ClpD, which is a member of the Clp protease system. Among the downregulated genes, five were homologous to serine peptidases and four were homologous to Arabidopsis Clp subunits (three homologous to Clp AAA+ chaperones and one to a ClpP-related ClpR subunit). Although the roles of serine peptidase inhibitors in plant defenses against herbivory have been extensively investigated, the roles of plant serine peptidases and the Clp protease system represent a new and underexplored field of study. The up- and downregulated D. saccharalis genes presented in this study may be candidate genes for the further investigation of the sugarcane response to herbivory.
Subject: Macroarray
Diatraea Saccharalis
Serine Peptidase Inhibitors
Serine Peptidase
Clp Protease System
Induced Resistance
Plant-insect Interaction
Editor: MDPI AG
Citation: International Journal Of Molecular Sciences. Mdpi Ag, v. 17, p. , 2016.
Rights: aberto
Identifier DOI: 10.3390/ijms17091444
Date Issue: 2016
Appears in Collections:Unicamp - Artigos e Outros Documentos

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