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Atomic force microscopy proposes a novel model for stem-loop structure that binds a heat shock protein in the Staphylococcus aureus HSP70 operon.
Ohta, T; Nettikadan, S; Tokumasu, F; Ideno, H; Abe, Y; Kuroda, M; Hayashi, H; Takeyasu, K.
Afiliação
  • Ohta T; Department of Microbiology, University of Tsukuba, Ibaraki, Japan.
Biochem Biophys Res Commun ; 226(3): 730-4, 1996 Sep 24.
Article em En | MEDLINE | ID: mdl-8831682
ABSTRACT
The Staphylococcus aureus HSP70 operon produces a polycistronic RNA in response to heat shock, and ORF37 is the first protein to be translated. The promoter of this operon contains a palindromic nucleotide sequence that may form a stem-loop structure. Structural analysis of the promoter regions by atomic force microscopy (AFM) revealed a quadruplet that consists of a pair of stem-loops. A novel "SL2S' (Stem-Loop-Loop-Stem) model was proposed for this structure. AFM also revealed the binding of ORF37 to the quadruplet, establishing a molecular mechanism for this heat shock gene expression; ORF37 acts as a regulator by binding to the SL2S structure in the promoter.
Assuntos
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Base de dados: MEDLINE Assunto principal: Óperon / Staphylococcus aureus / DNA Bacteriano / Proteínas de Choque Térmico HSP70 / Conformação de Ácido Nucleico Idioma: En Ano de publicação: 1996 Tipo de documento: Article
Buscar no Google
Base de dados: MEDLINE Assunto principal: Óperon / Staphylococcus aureus / DNA Bacteriano / Proteínas de Choque Térmico HSP70 / Conformação de Ácido Nucleico Idioma: En Ano de publicação: 1996 Tipo de documento: Article