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The sequences of MinE responsible for its subcellular localization analyzed by competitive binding method in Escherichia coli.
Pérez-Rodríguez, Miguel Á; Rodríguez-Luna, Isabel Cristina; Carreño-López, Ricardo; Lara-Ramírez, Edgar E; Rodríguez-Pérez, Mario A; Guo, Xianwu.
Afiliação
  • Pérez-Rodríguez MÁ; Departamento de Botánica, Universidad Autónoma Agraria Antonio Narro, Saltillo, Coahuila, Mexico.
  • Rodríguez-Luna IC; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Boulevard del Maestro S/N esquina Elías piña. Colonia Narciso Mendoza, 88710, Cd. Reynosa, Tamaulipas, Mexico.
  • Carreño-López R; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Boulevard del Maestro S/N esquina Elías piña. Colonia Narciso Mendoza, 88710, Cd. Reynosa, Tamaulipas, Mexico.
  • Lara-Ramírez EE; Centro de Investigaciones en Ciencias Microbiológicas, Benemérita Universidad Autónoma de Puebla, Puebla, Mexico.
  • Rodríguez-Pérez MA; Unidad de Investigación Biomédica de Zacatecas, Instituto Mexicano del Seguro Social (IMSS), Zacatecas, Mexico.
  • Guo X; Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Boulevard del Maestro S/N esquina Elías piña. Colonia Narciso Mendoza, 88710, Cd. Reynosa, Tamaulipas, Mexico.
Int Microbiol ; 21(1-2): 15-22, 2018 Jun.
Article em En | MEDLINE | ID: mdl-30810919
The subcellular localization of a protein is important for its proper function. Escherichia coli MinE is a small protein with clear subcellular localization, which provides a good model to study protein localization mechanism. In the present study, a series of recombinant minEs truncated in one end or in the middle regions, fused with egfp, was constructed, and these recombinant proteins could compete to function with the chromosomal MinE. Our results showed that the sequences related to the subcellular localization of MinE span several functional domains, demonstrating that MinE positioning in cells depends on multiple factors. The eGFP fusions with some truncated MinE from N-terminal resulted in different cell phenotypes and localization features, implying that these fusions can interfere chromosomal MinE's function, similar to MinE36-88 phenotype in the previous report. The amino acid in the region (32-48) is sensitive to change MinE conformation and influence its dimerization. Some truncated protein structure could be unstable. Thus, the MinE localization is prerequisite for its proper anti-MinCD function and some new features of MinE were demonstrated. This approach can be extended for subcellular localization research for other essential proteins.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Ciclo Celular / Proteínas de Escherichia coli / Mapeamento de Interação de Proteínas / Escherichia coli Tipo de estudo: Evaluation_studies / Prognostic_studies Idioma: En Revista: Int Microbiol Assunto da revista: MICROBIOLOGIA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: México País de publicação: Suíça
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Ciclo Celular / Proteínas de Escherichia coli / Mapeamento de Interação de Proteínas / Escherichia coli Tipo de estudo: Evaluation_studies / Prognostic_studies Idioma: En Revista: Int Microbiol Assunto da revista: MICROBIOLOGIA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: México País de publicação: Suíça