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Nucleotide signaling pathway convergence in a cAMP-sensing bacterial c-di-GMP phosphodiesterase.
Cadby, Ian T; Basford, Sarah M; Nottingham, Ruth; Meek, Richard; Lowry, Rebecca; Lambert, Carey; Tridgett, Matthew; Till, Rob; Ahmad, Rashidah; Fung, Rowena; Hobley, Laura; Hughes, William S; Moynihan, Patrick J; Sockett, R Elizabeth; Lovering, Andrew L.
Affiliation
  • Cadby IT; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, UK.
  • Basford SM; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Nottingham R; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Meek R; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, UK.
  • Lowry R; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Lambert C; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Tridgett M; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, UK.
  • Till R; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Ahmad R; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Fung R; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Hobley L; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Hughes WS; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, UK.
  • Moynihan PJ; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, UK.
  • Sockett RE; Centre for Genetics and Genomics, School of Biology, Medical School, Queen's Medical Centre, Nottingham University, Nottingham, UK.
  • Lovering AL; Institute for Microbiology and Infection, School of Biosciences, University of Birmingham, Birmingham, UK.
EMBO J ; 38(17): e100772, 2019 09 02.
Article in En | MEDLINE | ID: mdl-31355487
Bacterial usage of the cyclic dinucleotide c-di-GMP is widespread, governing the transition between motile/sessile and unicellular/multicellular behaviors. There is limited information on c-di-GMP metabolism, particularly on regulatory mechanisms governing control of EAL c-di-GMP phosphodiesterases. Herein, we provide high-resolution structures for an EAL enzyme Bd1971, from the predatory bacterium Bdellovibrio bacteriovorus, which is controlled by a second signaling nucleotide, cAMP. The full-length cAMP-bound form reveals the sensory N-terminus to be a domain-swapped variant of the cNMP/CRP family, which in the cAMP-activated state holds the C-terminal EAL enzyme in a phosphodiesterase-active conformation. Using a truncation mutant, we trap both a half-occupied and inactive apo-form of the protein, demonstrating a series of conformational changes that alter juxtaposition of the sensory domains. We show that Bd1971 interacts with several GGDEF proteins (c-di-GMP producers), but mutants of Bd1971 do not share the discrete phenotypes of GGDEF mutants, instead having an elevated level of c-di-GMP, suggesting that the role of Bd1971 is to moderate these levels, allowing "action potentials" to be generated by each GGDEF protein to effect their specific functions.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cyclic AMP / Phosphoric Diester Hydrolases / Bdellovibrio bacteriovorus Language: En Journal: EMBO J Year: 2019 Document type: Article Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Cyclic AMP / Phosphoric Diester Hydrolases / Bdellovibrio bacteriovorus Language: En Journal: EMBO J Year: 2019 Document type: Article Country of publication: