Galls from Calliandra brevipes BENTH (Fabaceae : Mimosoidae): evidence of apyrase activity contribution in a plant–insect interaction
Michelle de Lima Detoni A F , Priscila Faria-Pinto A , Leonardo Ramos Quellis A , Naiara Miranda Rust A , Letícia Stephan Tavares A , Marcelo de Oliveira Santos A , Rosy Mary dos Santos Isaias B , Jean Carlos Santos C , G. Wilson Fernandes D , Geraldo Luiz Gonçalves Soares E and Eveline Gomes Vasconcelos A
+ Author Affiliations
- Author Affiliations
A Departamento de Bioquímica and Departamento de Biologia, Pós-Graduação em Ciências Biológicas (Genética e Biotecnologia), ICB, Universidade Federal de Juiz de Fora, Campus Universitário, Bairro Cidade Universitária, Juiz de Fora, MG 36036-330, Brazil.
B Departamento de Botânica, ICB, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
C Instituto de Biologia, Universidade Federal de Uberlândia, Uberlândia, MG, Brazil.
D Ecologia Evolutiva and Biodiversidade/DBG, ICB, Universidade Federal de Minas Gerais, Belo Horizonte, MG, Brazil.
E Departamento de Botânica, IB, Universidade Federal do Rio Grande do Sul, Porto Alegre, RS, Brazil.
F Corresponding author. Email: michelledetoni@yahoo.com.br
Australian Journal of Botany 60(6) 559-567 https://doi.org/10.1071/BT12096
Submitted: 25 April 2012 Accepted: 4 July 2012 Published: 20 September 2012
Abstract
By western blots, cross-immunoreactivity with polyclonal anti-potato apyrase antibodies identified the Calliandra brevipes apyrase as a band of 75 kDa in the tissues of non-galled stem and leaves, and those of globose galls. The non-galled tissues hydrolysed either ATP, ADP, UDP, GTP or GDP. In globose galls, ADP, UDP and GDP hydrolysis were 1.7–5.1-fold higher than in non-galled tissues. ADP and UDP hydrolysis either from non-galled or globose gall tissues were 10–38% stimulated by 5 mM calcium, and drastically reduced (66–99%) by the addition of 5 mM EDTA or EGTA, confirming the divalent cation dependence. Nucleotidase, phosphatase or ATPase activities contributed in lower reaction rates. Apyrase activity was confirmed in C. brevipes tissues by nondenaturing polyacrylamide gel electrophoresis and western blots. By histochemical techniques, the ADPase activity was found as a granular-dense lead phosphate deposit homogeneously distributed at the external surface, and inside the nutritive cells of the globose gall. The sites of polyclonal anti-potato apyrase antibodies corroborate these localisations. The globose galls of the C. brevipes stems increase their capacity of hydrolysing nucleotides, which could be associated with carbohydrate biosynthesis, signalling and/or cell proliferation, crucial for feeding and survival of the insect.
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