Laboratory for Advanced Biomolecular Engineering

Research Summary

We are engineering functional biomacromolecules applicable to medical and basic researches, by integrating technologies in synthetic and structural biology including peptide/RNA in vitro evolution, X-ray crystallography, etc. Utilizing the same technologies, we are also trying to reconstruct the evolutional pathway of primordial proteins.

Research Theme

• We are engineering peptides that control cells and enzymes for use in medical and basic science.
• We are trying to experimentally reconstruct evolutional pathway from primordial peptides to elaborate proteins.

Main Publications List

• Tagami S, Attwater J, Holliger P.
  Simple peptides derived from the ribosomal core potentiate RNA polymerase ribozyme function.
  Nature Chemistry 9. 325-332 (2017) doi: 10.1038/nchem.2739.
• Tagami S, Sekine S, Minakhin L, et al.
  Structural basis for promoter specificity switching of RNA polymerase by a phage factor.
  Genes & Development 28(5). 521-531 (2014) doi: 10.1101/gad.233916.113
• Attwater J, Tagami S, Kimoto M, et al.
  Chemical fidelity of an RNA polymerase ribozyme.
  Chemical Science 4. 2804–2814 (2013) doi: 10.1039/C3SC50574J
• Sekine S, Tagami S, Yokoyama S
  Structural basis of transcription by bacterial and eukaryotic RNA polymerases.
  Current Opinion in Structural Biology 22(1). 110-118 (2012) doi: 10.1016/j.sbi.2011.11.006
• Tagami S, Sekine S, Yokoyama S.
  A novel conformation of RNA polymerase sheds light on the mechanism of transcription.
  Transcription 2(4). 162-167 (2011) doi: 10.4161/trns.2.4.16148
• Tagami S, Sekine S, Kumarevel T, et al.
  Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein.
  Nature 468(7326). 978-982 (2010) doi: 10.1038/nature09573
• Tagami S, Sekine S, Kumarevel T, et al.
  Crystallization and preliminary X-ray crystallographic analysis of Thermus thermophilus transcription elongation complex bound to Gfh1.
  Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS 66(Pt1). 63-68 (2010) doi: 10.1038/nature09573

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