Sugarcane Serine Peptidase Inhibitors, Serine Peptidases, and Clp Protease System Subunits Associated with Sugarcane Borer (Diatraea saccharalis) Herbivory and Wounding.
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.
Departamento de Ciências da Natureza, Matemática e Educação, Universidade Federal de São Carlos, Araras, 13600-970 São Paulo, Brazil. anehm@cca.ufscar.br.|Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, 13418-260 São Paulo, Brazil. anehm@cca.ufscar.br.
Ane H
AH
Medeiros
Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, 13418-260 São Paulo, Brazil. fabiana.mingossi@gmail.com.
Fabiana B
FB
Mingossi
Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, 13418-260 São Paulo, Brazil. diasrdo@gmail.com.
Renata O
RO
Dias
Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, 13418-260 São Paulo, Brazil. flavia.esalq@gmail.com.
Flávia P
FP
Franco
Systems Biology Laboratory, Center for Molecular Biology and Genetic Engineering, State University of Campinas, Campinas, 13083-970 São Paulo, Brazil. shinapes@unicamp.br.
Renato
R
Vicentini
Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, 13418-260 São Paulo, Brazil. marcia.o.jose@gmail.com.|Monsanto do Brasil, Campinas, 13069-380 São Paulo, Brazil. marcia.o.jose@gmail.com.
Marcia O
MO
Mello
Departamento de Ciências Biológicas, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, 13400-918 São Paulo, Brazil. danielmoura@usp.br.
Daniel S
DS
Moura
Departamento de Genética, Escola Superior de Agricultura Luiz de Queiroz, Universidade de São Paulo, Piracicaba, 13418-260 São Paulo, Brazil. mdcsilva@usp.br.
Marcio C
MC
Silva-Filho
D000818:Animals; D015536:Down-Regulation; D049071:Endopeptidase Clp / Q000235:genetics / Q000378:metabolism*; D006790:Host-Parasite Interactions / Q000235:genetics*; D007915:Lepidoptera / Q000472:pathogenicity*; D010802:Phylogeny; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism; D031786:Saccharum / Q000201:enzymology* / Q000235:genetics / Q000469:parasitology; D015842:Serine Proteinase Inhibitors / Q000378:metabolism*
D010940:Plant Proteins; D021122:Protein Subunits; D015842:Serine Proteinase Inhibitors; D049071:Endopeptidase Clp
Clp protease system; Diatraea saccharalis; induced resistance; macroarray; plant–insect interaction; serine peptidase; serine peptidase inhibitors; sugarcane