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Phosphorylation status of BolA affects its role in transcription and biofilm development.
Galego, Lisete; Barahona, Susana; Romão, Célia V; Arraiano, Cecília M.
Afiliação
  • Galego L; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
  • Barahona S; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
  • Romão CV; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
  • Arraiano CM; Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Oeiras, Portugal.
FEBS J ; 288(3): 961-979, 2021 02.
Article em En | MEDLINE | ID: mdl-32535996
ABSTRACT
BolA has been characterized as an important transcriptional regulator, which is induced in stationary phase of growth, and in response to several stresses. In Escherichia coli, its cellular function is associated with cell wall synthesis and division, morphology, permeability, motility and biofilm formation. Phosphorylation has been widely described as one of the most important events involved in the modulation of the activity of many transcription factors. In the present work, we have demonstrated in vivo and by mass spectrometry that BolA is phosphorylated in four highly conserved protein positions S26, S45, T81 and S95. S95 is located in the C terminus unstructured region of the protein, and the other three sites are in the DNA-binding domain. These positions were mutated to nonphosphorylated residues, and their effects were investigated on different known BolA functions. Using northern blot experiments, we showed that the regulation of the expression of these Ser/Thr BolA mutants is performed at the post-translational level. Western blot results revealed that the stability/turnover of the mutated BolA proteins is differently affected depending on the dephosphorylated residue. Moreover, we provide evidences that phosphorylation events are crucial in the modulation of BolA activity as a transcription factor and as a regulator of cell morphology and biofilm development. Here, we propose that phosphorylation affects BolA downstream functions and discuss the possible significance of these phosphoresidues in the protein structure, stability, dimerization and function as a transcription factor.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fatores de Transcrição / Regulação Bacteriana da Expressão Gênica / Biofilmes / Proteínas de Escherichia coli / Escherichia coli Idioma: En Revista: FEBS J Assunto da revista: BIOQUIMICA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Portugal

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fatores de Transcrição / Regulação Bacteriana da Expressão Gênica / Biofilmes / Proteínas de Escherichia coli / Escherichia coli Idioma: En Revista: FEBS J Assunto da revista: BIOQUIMICA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Portugal