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A division of labor between two biotin protein ligase homologs.
Song, Xuejiao; Henke, Sarah K; Cronan, John E.
Afiliação
  • Song X; Department of Biochemistry, University of Illinois, Urbana, IL, USA.
  • Henke SK; Department of Microbiology, University of Illinois, Urbana, IL, USA.
  • Cronan JE; Department of Biochemistry, University of Illinois, Urbana, IL, USA.
Mol Microbiol ; 116(2): 648-662, 2021 08.
Article em En | MEDLINE | ID: mdl-34028100
Group I biotin protein ligases (BPLs) catalyze the covalent attachment of biotin to its cognate acceptor proteins. In contrast, Group II BPLs have an additional N-terminal DNA-binding domain and function not only in biotinylation but also in transcriptional regulation of genes of biotin biosynthesis and transport. Most bacteria contain only a single biotin protein ligase, whereas Clostridium acetobutylicum contains two biotin protein ligase homologs: BplA and BirA'. Sequence alignments showed that BplA is a typical group I BPL, whereas BirA' lacked the C-terminal domain conserved throughout extant BPL proteins. This raised the questions of why two BPL homologs are needed and why the apparently defective BirA' has been retained. We have used in vivo and in vitro assays to show that BplA is a functional BPL whereas BirA' acts as a biotin sensor involved in transcriptional regulation of biotin transport. We also successfully converted BirA' into a functional biotin protein ligase with regulatory activity by fusing it to the C-terminal domain from BplA. Finally, we provide evidence that BplA and BirA' interact in vivo.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Transcrição Gênica / Biotina / Carbono-Nitrogênio Ligases / Biotinilação / Clostridium acetobutylicum Idioma: En Revista: Mol Microbiol Assunto da revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Transcrição Gênica / Biotina / Carbono-Nitrogênio Ligases / Biotinilação / Clostridium acetobutylicum Idioma: En Revista: Mol Microbiol Assunto da revista: BIOLOGIA MOLECULAR / MICROBIOLOGIA Ano de publicação: 2021 Tipo de documento: Article País de afiliação: Estados Unidos