title: A two-dimensional electrophoretic profile of the proteins secreted by Herbaspirillum seropedicae strain Z78.
abstract: Herbaspirillum seropedicae is an endophytic bacterium that associates with rice, sugarcane and other economically important crops. Secreted proteins play a key role in the plant-bacterial interaction. Using 2D electrophoresis and peptide mass fingerprint mass spectrometry, 63 protein spots representing 41 different secreted proteins were identified during growth of H. seropedicae under nitrogen-sufficient conditions. In silico analysis showed that 25.4% of the proteins had signal peptides and 15.9% were predicted to be non-classically secreted. Among the most abundant were flagellar components and ABC-type transport system proteins. Nine secreted proteins had also been identified in the cellular proteome, suggesting that they also play a role in the extracellular environment. No type III secreted proteins were detected by comparison of the wild type strain with an hrcN mutant strain.
authors: Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Paraná, C. Postal 19046, 81531-990, Curitiba, PR, Brazil.
authors: Daniela Fojo Seixas
authors: DF
authors: Chaves
authors: Emanuel Maltempi
authors: EM
authors: de Souza
authors: Rose Adele
authors: RA
authors: Monteiro
authors: Fábio
authors: F
authors: de Oliveira Pedrosa
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis* / Q000378:metabolism*; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods; D042803:Herbaspirillum / Q000378:metabolism*; D030781:Organisms, Genetically Modified; D020543:Proteome / Q000032:analysis / Q000378:metabolism; D040901:Proteomics / Q000379:methods; D013045:Species Specificity
chemical_list: D001426:Bacterial Proteins; D020543:Proteome