RIKEN Center for Life Science Technologies


  • Research

    Latest publications from CLST.
  • News

    Awards, agreements, and other news.
  • Events

    Upcoming and past events including seminars, symposiums, open days.

For Public

To let you know about our research, this area contains 4 types of information about CLST; “Article”, “Videos”, “Event” and “Study”.
At “Article”, you can read articles on interviews and lectures, and you can enjoy the videos about CLST at “Videos”. If you want to meet and talk directly with the researcher, “Visit” give you some information of such events. You can find more difficult contents to know about our research deeply at “Study”.
  • Article
  • Event
  • Videos
  • Study

Labs & Technologies

Nonnatural Amino Acid Technology Team

We bring about superproteins.


* Due to the reorganization starting as new centers in April 2018, this laboratory is now belong to the Center for Biosystems Dynamics Research. As for the latest information, please see the following URL below.
> The webpage of Laboratory for Nonnatural Amino Acid Technology, Center for Biosystems Dynamics Research

Team Leader
Kensaku Sakamoto  Ph.D.

Room W223, West Building, 1-7-22 Suehiro-cho,Tsurumi-ku, Yokohama 230-0045
Tel: +81-45-503-9459


Research Area

What is Synthetic biology?

 Proteins useful for life-science studies and medical applications can be synthesized in living cells programmed with the blueprint for the proteins. The cells engineered to utilize novel amino acids in proteins will facilitate the addition of artificial marks onto proteins, and also the synthesis of proteins linked to pharmaceuticals. These cells will help to realize new structures and functions of proteins. We also exploit this platform technology to provide unique, technical supports for drug discovery.

Collaborations with Structural Biology

Synthetic Biology should work together with Structural Biology, to develop novel proteins and enzymes based on structural knowledge. Not only for engineering, has such collaboration proved useful for elucidating structural basis for the functions of proteins, receptors, and enzymes. 

Main Publications List


Ubiquitin acetylation inhibits polyubiquitin chain elongation.

Ohtake F, Saeki Y, Sakamoto K, Ohtake K, Nishikawa H, Tsuchiya H, Ohta T, Tanaka K, and Kanno J.
EMBO Rep, 16(2), 192-201 (2015).

Efficient decoding of the UAG triplet as a full-fledged sense codon enhances the growth of a prfA-deficient strain of Escherichia coli.

Ohtake K, Sato A, Mukai T, Hino N, Yokoyama S, Sakamoto K.
J Bacteriol, 194(10), 2606-2613 (2012).

Dissecting cell signaling pathways with genetically encoded 3-iodo-L-tyrosine

Hayashi A, Hino N, Kobayashi T, Arai R, Shirouzu M, Yokoyama S, Sakamoto K.
Chembiochem, 12(3), 387-389 (2011).

Crystallographic study of a site-specifically cross-linked protein complex with a genetically incorporated photoreactive amino acid.

Sato S, Mimasu S, Sato A, Hino N, Sakamoto K, Umehara T, Yokoyama S.
Biochemistry, 50(2), 250-257 (2011).

Crystal structure of bacterial RNA polymerase bound with a transcription inhibitor protein.

Tagami S, Sekine S, Kumarevel T, Hino N, Murayama Y, Kamegamori S, Yamamoto M, Sakamoto K, Yokoyama S.
Nature, 468(7326), 978-982 (2010).

Codon reassignment in the Escherichia coli genetic code

Mukai T, Hayashi A, Iraha F, Sato A, Ohtake K, Yokoyama S, Sakamoto K.
Nucleic Acids Res, 38(22), 8188-8195 (2010).

Functional replacement of the endogenous tyrosyl-tRNA synthetase-tRNATyr pair by the archaeal tyrosine pair in Escherichia coli for genetic code expansion.

Iraha F, Oki K, Kobayashi T, Ohno S, Yokogawa T, Nishikawa K, Yokoyama S, Sakamoto K.
Nucleic Acids Res, 38(11), 3682-3691 (2010).

Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog

Oki K, Sakamoto K, Kobayashi T, Sasaki HM, Yokoyama S.
Proc Natl Acad Sci U S A, 105(36), 13298-13303 (2008).

Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid

Hino N, Okazaki Y, Kobayashi T, Hayashi A, Sakamoto K, Yokoyama S.
Nat Methods, 2(3), 201-206 (2005).

>>>ALL Publications

Member  *concurrent

CLST was reorganized into three centers according to the RIKEN 4th Medium-Term Plan from April 1, 2018. For the latest information of Nonnatural Amino Acid Technology Team, please visit the following websites.

> The webpage of Laboratory for Nonnatural Amino Acid Technology, Center for Biosystems Dynamics Research [http://www.bdr.riken.jp/en/research/labs/sakamoto-k/index.html]