Meloidogyne incognita: molecular cloning and characterization of a cDNA encoding a cathepsin D-like aspartic proteinase
Autor: | Fragoso, Rodrigo da Rocha, Lourenço, Isabela Tristan, Batista, João Aguiar Nogueira, Oliveira-Neto, Osmundo Brilhante, Silva, Maria Cristina Mattar, Rocha, Thales Lima, Coutinho, Marise Ventura, Grossi-de-Sa, Maria Fátima |
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Jazyk: | angličtina |
Rok vydání: | 2009 |
Předmět: | |
Zdroj: | Repositório Institucional da UCB Universidade Católica de Brasília (UCB) instacron:UCB |
Popis: | Made available in DSpace on 2016-10-10T03:52:21Z (GMT). No. of bitstreams: 5 Meloidogyne incognita_molecular cloning and characterization.PDF: 1058825 bytes, checksum: 149f0214de61c9c6736076381cd2c9e5 (MD5) license_url: 52 bytes, checksum: 2f32edb9c19a57e928372a33fd08dba5 (MD5) license_text: 24259 bytes, checksum: f1f24f769b03eb8f9cd3f53c1090841c (MD5) license_rdf: 24658 bytes, checksum: 9d3847733d3c0b59c7c89a1d40d3d240 (MD5) license.txt: 1887 bytes, checksum: 445d1980f282ec865917de35a4c622f6 (MD5) Previous issue date: 2009 Herein we describe the cloning and characterization of a cDNA encoding an aspartic proteinase from the root-knot nematode Meloidogyne incognita. Using PCR techniques, a 1471-bp cDNA fragment encoding a cathepsin D-like (Mi-asp1) transcript was isolated from second- stage larvae mRNA. Its predicted amino acid sequence comprises a pro-region of 71 amino acid residues and a mature protease of 378 amino acid residues with a predicted molecular mass of 41.502 kDa. Protein sequence comparisons of Mi-asp1 with GenBank ™ (DQ360827) sequences showed 59–71% identity with nematode- specific cathepsin D-like aspartic proteinases. Southern blot analysis, RT-PCR amplification and EST mining suggest the existence of a developmentally expressed gene family encoding aspartic proteinases in M. incognita. Mi-asp1 may represent a potential target for molecular intervention for the purposes of plant–parasitic nematode control. Sim Publicado |
Databáze: | OpenAIRE |
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