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Life and Coordination-Complex Molecular Science Aono Group

Aono Group -main_image
Location: Yamate, No.2 Bldg.3F east Room3
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Bioinorganic Chemistry, Metalloproteins, Sensor Protein

Bioinorganic Chemistry of Metalloproteins Responsible for Signal Transduction

Transition metal ions and metalloproteins play crucial roles in signal transduction processes in addition to their traditional roles in energy and substance metabolisms. Many responses to metals occur transcriptionally or post-transcriptionally. The metal-responsive transcription factors control the expression of genes encoding proteins responsible for metal homeostasis in cells including metal ions uptake/efflux, intracellular metal trafficking, and biogenesis of metalloproteins. Metal-responsive signal transduction pathways emanating from metal sensing at the cell membrane are also responsible for biological regulation in response to metals. Metal-based sensor proteins are utilized to sense external signals that cannot be sensed by simple sensor proteins without any prosthetic group, in which transition metal ions or metal-containing prosthetic groups act as the active center of signal sensing.  

My research interests are foucused on the elucidation of the structural and functional relationships for metal-dependent proteins working in biological signal-transduction systems including metal-based sensor proteins, transition metal ion-sensing transcriptional regulators, and protein machineries responsible for metal ions homeostasis in both prokaryotes and eukaryotes.

160309.jpgX-ray crystal structure of N-terminal domain of HtaA responsible for heme uptake in C. glutamicum (left) and a close-up view of its heme-binding pocket (right).

Selected Publications

  1. “Protein Dynamics of the Sensor Protein HemAT as Probed by Time-Resolved Step-Scan FTIR Spectroscopy,” A. Pavlou, H. Yoshimura, S. Aono, E. Pinakoulaki, Biophys. J. 114, 584-591 (2018).
  2. “Probing the role of the heme distal and proximal environment in ligand dynamics in the signal transducer protein HemAT by time-resolved step-scan FTIR and  resonance Raman spectroscopy,” A. Pavlou, A. Loullis, H. Yoshimura, S. Aono, E. Pinakoulaki, Biochemistry, 56, 5309-5317 (2017). 
  3. “Structural characterization of heme environmental mutants of CgHmuT that shuttles heme molecules to heme transporters,” N. Muraki, C. Kitatsugi, M. Ogura, T. Uchida, K. Ishimori, S. Aono, Int. J. Mol. Sci.17, 829 (10pages) (2016).
  4. “Structural Basis for Heme Recognition by HmuT Responsible for Heme Transport to the Heme Transporter in Corynebacterium glutamicum,” N. Muraki, S. Aono, Chem. Lett.45, 24-26 (2015).
  5. “Heme-binding properties of HupD functioning as a substrate-binding protein in a heme-uptake ABC-transporter system in Listeria monocytogenes,” Y. Okamoto, H.
    Sawai, M. Ogura, T. Uchida, K. Ishimori, T. Hayashi, S. Aono, Bull. Chem. Soc. Jpn.87, 1140-1146 (2014).
  6. “The Dos family of globin-related sensors using PAS domains to accommodate haem acting as the active site for sensing external signals,” S. Aono, Adv. Microbial Physiol.63, 273-327 (2013).