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Evidence for glycosylation on a DNA-binding protein of <Emphasis Type="Italic">Salmonella enterica</Emphasis>
Authors:Ebert S Hanna  Maria-Cristina Roque-Barreira  Emerson S Bernardes  Ademilson Panunto-Castelo  Marcelo V Sousa  Igor C Almeida  Marcelo Brocchi
Institution:1.Departamento de Biologia Celular e Molecular e Bioagentes Patogênicos,Faculdade de Medicina de Ribeir?o Preto, Universidade de S?o Paulo,Ribeir?o Preto,Brazil;2.Departamento de Enfermagem Geral e Especializada,Escola de Enfermagem de Ribeir?o Preto, Universidade de S?o Paulo,Ribeir?o Preto,Brazil;3.Centro Brasileiro para Pesquisas e Servi?os em Proteinas, Instituto de Biologia,Universidade de Brasília,Brasília,Brazil;4.Department of Biological Sciences,University of Texas at El Paso,USA;5.Departmento de Microbiologia e Imunologia,Instituto de Biologia, Rua Charles Darwin s/n, UNICAMP,Campinas,Brazil
Abstract:

Background  

All organisms living under aerobic atmosphere have powerful mechanisms that confer their macromolecules protection against oxygen reactive species. Microorganisms have developed biomolecule-protecting systems in response to starvation and/or oxidative stress, such as DNA biocrystallization with Dps (DNA-binding protein from starved cells). Dps is a protein that is produced in large amounts when the bacterial cell faces harm, which results in DNA protection. In this work, we evaluated the glycosylation in the Dps extracted from Salmonella enterica serovar Typhimurium. This Dps was purified from the crude extract as an 18-kDa protein, by means of affinity chromatography on an immobilized jacalin column.
Keywords:
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