RIKEN Center for Life Science Technologies


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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”.
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Labs & Technologies

Supramolecular Structural Biology Team

Be pioneering.


* 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 Transcription Structural Biology, Center for Biosystems Dynamics Research

Team Leader
Shun-ichi Sekine  Ph.D.

1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, 230-0045 JAPAN (W219)


Research Area

We plan to conduct structural biology studies to unravel action mechanisms of cellular macromolecular systems comprising DNAs, RNAs, and proteins, typified by various complexes of RNA polymerases bound with nucleic acids and transcription factors. To this end, we will develop a technology platform for the supramolecular structure analysis, with novel methods for the preparation of biologically significant macromolecular complexes consisting of a number of large components and for the structure analysis by taking advantage of SPring-8/SACLA and other spectroscopic methods.

Cryo-EM density map of the RNA polymerase II elongation complex (left).  Structure of the RNA polymerase II elongation complex bound with Spt4, Spt5, Elf1, and TFIIS, revealed by cryo-EM and X-ray crystallography (right).

Main Publications List


The ratcheted and ratchetable structural states of RNA polymerase underlie multiple transcriptional functions

Sekine S, Murayama Y, Svetlov V, Nudler E, Yokoyama S.
Mol Cell, 57(3), 408-421 (2015).

Development of a hexahistidine-3× FLAG-tandem affinity purification method for endogenous protein complexes in Pichia pastoris.

Higo T, Suka N, Ehara H, Wakamori M, Sato S, Maeda H, Sekine S, Umehara T, Yokoyama S.
J Struct Funct Genomics, 15(4), 191–199 (2014).

The selective tRNA aminoacylation mechanism based on a single G•U pair

Naganuma M, Sekine S, Chong YE, Guo M, Yang XL, Gamper H, Hou YM, Schimmel P, Yokoyama S
Nature, 510(7506), 507-511 (2014).

Structural basis for promoter specificity switching of RNA polymerase by a phage factor

Tagami S, Sekine S, Minakhin L, Esyunina D, Akasaka R, Shirouzu M, Kulbachinskiy A, Severinov K, Yokoyama S.
Genes Dev, 28(5), 521-531 (2014).

Decameric SelA•tRNASec Ring Structure Reveals Mechanism of Bacterial Selenocysteine Formation

Itoh Y, Brocker MJ, Sekine S, Hammond G, Suetsugu S, Soll D, Yokoyama S.
Science, 340(6128), 75-78 (2013).

Crystallization and preliminary X-ray crystallographic analyses of Thermus thermophilus backtracked RNA polymerase.

Murayama Y, Sekine S, Yokoyama S.
Acta Crystallogr Sect F-Struct Biol Cryst Commun, 69(Pt2), 174-177 (2013).

Structural basis of transcription by bacterial and eukaryotic RNA polymerases.

Sekine S, Tagami S, Yokoyama S.
Curr Opin Struct Biol, 22(1), 110-118 (2012).

Crystal structure of the C17/25 subcomplex from Schizosaccharomyces pombe RNA polymerase III.

Ehara H, Sekine S, Yokoyama S.
Protein Sci, 20(9), 1558-1565 (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).

Member  *concurrent

  • >>>Curriculum vitae

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

> The webpage of Laboratory for Transcription Structural Biology, Center for Biosystems Dynamics Research [http://www.bdr.riken.jp/en/research/labs/sekine-s/index.html]