Kiyoshi Nagai

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This article is about the Japanese biologist. For the Japanese manga artist, see Go Nagai.
Kiyoshi Nagai
FRS
Kiyoshi Nagai, November 2018
Born(1949-06-25)June 25, 1949
Osaka, Japan
DiedSeptember 27, 2019(2019-09-27) (aged 70)
Cambridge, United Kingdom
NationalityJapanese
Alma materOsaka University (BSc, MSc, PhD)
Awards
  • EMBO Member
    (2000)
  • Novartis Medal and Prize
    (2000)
Scientific career
InstitutionsMRC Laboratory of Molecular Biology
Thesis (1978)
Doctoral advisorHideki Morimoto
Websitewww2.mrc-lmb.cam.ac.uk/group-leaders/n-to-s/kiyoshi-nagai/

Kiyoshi Nagai FRS (June 25, 1949 – September 27, 2019) was a Japanese structural biologist at the MRC Laboratory of Molecular Biology Cambridge, UK. He was known for his work on the mechanism of RNA splicing and structures of the spliceosome.

Education

Nagai studied at Osaka University and earned a Doctor of Philosophy under the supervision of Hideki Morimoto working on the allosteric effect in hemoglobin.[1]

Career and research

In 1981 Nagai moved to the

MRC Laboratory of Molecular Biology where he worked as a post-doc with Max Perutz on overproduction of eukaryotic proteins in E. coli.[1] He produced recombinant hemoglobin and studied its properties and evolution by crystallography and mutagenesis.[2][3] In 1987 he became a tenured group leader at the LMB and was joint head of the Division of Structural Studies from 2000 to 2010. He was appointed fellow of Darwin College, Cambridge in 1993.[4]

In 1990 his group solved the first structure of an RRM (RNA recognition motif) protein, U1A,[5] and in 1994 showed how it specifically binds RNA.[6] Subsequent work involved crystallographic studies of other components of the spliceosome, a large macromolecular machine that catalyses RNA splicing in eukaryotes, including components of the U2 snRNP[7] and the Sm proteins[8] and culminating in the crystal structures of the full U1 snRNP[9][10] and the U5 snRNP components Prp8[11] and Brr2.[12]

From 2014, Nagai's group used cryo-electron microscopy to study the spliceosome. Structures of the U5.U4/U6 tri-snRNP gave the first structural insights into the assembly of the spliceosome.[13][14] Nagai's subsequent structures of spliceosomes in various stages of assembly and catalysis[15][16] combined with structures from the groups of Reinhard Lührmann, Yigong Shi and others have provided crucial insight into the catalytic mechanism of pre-mRNA splicing.

Awards

References

  1. ^
    PMID 29377672
    .
  2. S2CID 4307749
    .
  3. PMID 3903751
    .
  4. ^ "Master & fellows | www.darwin.cam.ac.uk". www.darwin.cam.ac.uk. Retrieved 2018-12-09.
  5. S2CID 4336326
    .
  6. S2CID 9404488
    .
  7. S2CID 204999419
    .
  8. S2CID 17379935
    .
  9. PMID 19325628
    .
  10. PMID 25555158
    .
  11. PMID 23354046
    .
  12. PMID 23727230
    .
  13. PMID 26106855
    .
  14. PMID 26829225
    .
  15. PMID 28981077
    .
  16. PMID 28888105
    .
  17. ^ "Kiyoshi Nagai | Royal Society". royalsociety.org. Retrieved 2018-12-09.
  18. S2CID 247453651
    .
  19. ^ "Find people in the EMBO Communities". people.embo.org. Retrieved 2018-12-09.
  20. PMID 11356120
    .
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