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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Molecular characterization of a miraculin-like gene differentially expressed during coffee development and coffee leaf miner infestation

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Costa Mondego, Jorge Mauricio [1, 2] ; Duarte, Melina Pasini [1] ; Kiyota, Eduardo [3, 4] ; Martinez, Leandro [5] ; de Camargo, Sandra Rodrigues [1] ; De Caroli, Fernanda P. [6] ; Capela Alves, Beatriz Santos [7] ; Carmello Guerreiro, Sandra Maria [8] ; Vilela Oliva, Maria Luiza [6] ; Guerreiro-Filho, Oliveiro [9] ; Menossi, Marcelo [1]
Total Authors: 11
Affiliation:
[1] Univ Estadual Campinas, UNICAMP, Inst Biol, Lab Genoma Func, Dept Genet Evolucao & Bioagentes, BR-13084971 Campinas, SP - Brazil
[2] IAC, Ctr Pesquisa & Desenvolvimento Recursos Genet Veg, BR-13001970 Campinas, SP - Brazil
[3] Univ Estadual Campinas, UNICAMP, Ctr Biol Mol & Engn Genet, BR-13083875 Campinas, SP - Brazil
[4] Univ Estadual Campinas, UNICAMP, Inst Quim, BR-13084862 Campinas, SP - Brazil
[5] Univ Sao Paulo, Inst Fis Sao Carlos, Grp Cristalog, BR-13566590 Sao Carlos, SP - Brazil
[6] Univ Fed Sao Paulo, Dept Bioquim, BR-04044020 Sao Paulo - Brazil
[7] LNBio, BR-13083970 Campinas, SP - Brazil
[8] Univ Estadual Campinas, UNICAMP, Inst Biol, Dept Biol Vegetal, BR-13084971 Campinas, SP - Brazil
[9] IAC, Ctr Cafe Alcides Carvalho, BR-13012970 Campinas, SP - Brazil
Total Affiliations: 9
Document type: Journal article
Source: PLANTA; v. 233, n. 1, p. 123-137, JAN 2011.
Web of Science Citations: 15
Abstract

The characterization of a coffee gene encoding a protein similar to miraculin-like proteins, which are members of the plant Kunitz serine trypsin inhibitor (STI) family of proteinase inhibitors (PIs), is described. PIs are important proteins in plant defence against insects and in the regulation of proteolysis during plant development. This gene has high identity with the Richadella dulcifica taste-modifying protein miraculin and with the tomato protein LeMir; and was named as CoMir (Coffea miraculin). Structural protein modelling indicated that CoMir had structural similarities with the Kunitz STI proteins, but suggested specific folding structures. CoMir was up-regulated after coffee leaf miner (Leucoptera coffella) oviposition in resistant plants of a progeny derived from crosses between C. racemosa (resistant) and C. arabica (susceptible). Interestingly, this gene was down-regulated during coffee leaf miner herbivory in susceptible plants. CoMir expression was up-regulated after abscisic acid application and wounding stress and was prominent during the early stages of flower and fruit development. In situ hybridization revealed that CoMir transcripts accumulated in the anther tissues that display programmed cell death (tapetum, endothecium and stomium) and in the metaxylem vessels of the petals, stigma and leaves. In addition, the recombinant protein CoMir shows inhibitory activity against trypsin. According to the present results CoMir may act in proteolytic regulation during coffee development and in the defence against L. coffeella. The similarity of CoMir with other Kunitz STI proteins and the role of CoMir in plant development and plant stress are discussed. (AU)