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IMSUT & RCAST GCOE Program Seminar < Global Education
Seminar >

Date and Time: JULY 2&s_comma; 2009 17:00 - 18:00
Venue : 2nd building 2F large lecture room&s_comma; Inst. Med. Scei.&s_comma; Univ.Tokyo
(Nanboku line/Mita line Shirokanedai station)
Speaker: Dmitry G. Vassylyev
Position : Professor
Affiliation:Department of Biochemistry and Molecular Genetics&s_comma;
University of Alabama at Birmingham&s_comma;Schools of Medicine and Dentistry
(Country: USA)
Seminar Title:Structural studies of the bacterial transcription
machinery.
(Language: English)
Summary:
In the past years&s_comma; a large body of high resolution structural data
that allowed a detailed characterization of various bacterial
transcription intermediates was accumulated in (and published by) our
lab. So far&s_comma; we have determined the structures of the bacterial RNA
polymerase (RNAP) holoenzyme (Ref. 1) and its binary complexes with
the small molecule transcription regulators/inhibitors (ppGpp;
rifamycins&s_comma; Rifs; tagetitoxin&s_comma; Tgt; streptolydigin&s_comma; Stl; and
myxopyronin&s_comma; Myx) (Refs. 2-7). The recently determined structure of
the bacterial elongation complex (EC) in the substrate-free and
substrate-bound forms (Refs. 8&s_comma; 9) provided deep insight in many
basic mechanisms of transcription and implied a plausible model of
substrate loading that might be universal for all RNAPs. Importantly&s_comma;
obtaining well-diffracting EC crystals raised structural studies of
transcription on a higher level allowing for substantially deeper
understanding of the regulatory events and revealing the structural
details that in many cases could not be even predicted based on the
previously available data. In my talk&s_comma; I will present a summary and
the major conclusions of our past studies&s_comma; as well as the new
structural data we have recently obtained on the EC/Tgt&s_comma; EC/Tgt/
AMPcPP&s_comma; EC/ppGpp&s_comma; and EC/ppGpp/AMPcPP complexes.
References:
1. Vassylyev&s_comma; et al. (2002) Nature 417&s_comma; 712-719.
2. Artsimovitch&s_comma; et al. (2004) Cell 117&s_comma; 299-310.
3. Perederina&s_comma; et al. (2004) Cell 118&s_comma; 297-309.
4. Artsimovitch&s_comma; et al. (2005) Cell 122&s_comma; 351-363.
5. Temiakov&s_comma; et al. (2005) Mol Cell 19&s_comma; 655-666.
6. Vassylyev&s_comma; et al. (2005) Nature Struc. Mol. Biol. 12&s_comma;
1086-1093.
7. Belogurov&s_comma; et al. (2009) Nature 457&s_comma; 332-335.
8. Vassylyev&s_comma; et al. (2007a) Nature 448&s_comma;157-162.
9. Vassylyev&s_comma; et al. (2007b) Nature 448&s_comma;163-168.

Host:Osamu Nureki (Division of Structure Biology )&s_comma;
Koichi Ito (Division of Division of Molecular Biology )

************************************************
Sumiko Watanabe&s_comma; Ph.D
Division of Molecular and Developmental Biology&s_comma; Insisute of Medical
Science
University of Tokyo
108-8639 Japan
Shirokane-dai 4-6-1&s_comma; Minatoku&s_comma; Tokyo
Phone: 81-3-5449-5663
FAX: 81-3-5449-5474
http://www.ims.u-tokyo.ac.jp/moldev/
***************************************************



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