Abstract

To further dissect the folding mechanism of the Tetrahymena ribozyme, we are exploring, in collaboration with Dr. Williamson and his co-workers (currently at Scripps Institute), the folding of several ?fast-folding? mutants of the Tetrahymena thermophila group I intron. These mutations are of particular interest in that they are all located within the P4-P6 domain although they profoundly influence the folding of the catalytic core of the ribozyme. Dr. Williamson?s group has characterized the temperature and urea dependence of folding Hof these mutants, using their oligonucleotide-hybridization method, Hwhich probes the formation of helix P3 in the ribozyme. owever, this Happroach is unable to probe the fast transitions that can be followed Hby synchrotron footprinting. In order to measure the rates of folding Hof the rest of the 400 bases-long RNA, Martha Rook, a graduate student Hin Williamson?s lab conducted a preliminary series time-resolved x-ray footprinting experiments on these mutants in collaboration with the Resource Center.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-19
Application #
6491435
Study Section
Project Start
2001-09-01
Project End
2002-08-31
Budget Start
Budget End
Support Year
19
Fiscal Year
2001
Total Cost
Indirect Cost

  Institution

Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461

  Publications

Vongsvivut, Jitraporn; Fernandez, Jason; Ekgasit, Sanong et al. (2004) Characterization of supported cylinder-planar germanium waveguide sensors with synchrotron infrared radiation. Appl Spectrosc 58:143-51
Masip, Lluis; Pan, Jonathan L; Haldar, Suranjana et al. (2004) An engineered pathway for the formation of protein disulfide bonds. Science 303:1185-9
Huang, Raymond Y; Miller, Lisa M; Carlson, Cathy S et al. (2003) In situ chemistry of osteoporosis revealed by synchrotron infrared microspectroscopy. Bone 33:514-21
Rashidzadeh, Hassan; Khrapunov, Sergei; Chance, Mark R et al. (2003) Solution structure and interdomain interactions of the Saccharomyces cerevisiae ""TATA binding protein"" (TBP) probed by radiolytic protein footprinting. Biochemistry 42:3655-65
Uchida, Takeshi; Takamoto, Keiji; He, Qin et al. (2003) Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme. J Mol Biol 328:463-78
Taylor, Colleen M; Watton, Stephen P; Bryngelson, Peter A et al. (2003) Inner-sphere complexation of cobalt(II) 2,9-dimethyl-1,10-phenanthroline ([Co(neo)]2+) with commercial and sol-gel derived silica gel surfaces. Inorg Chem 42:312-20
Tang, Qun; Carrington, Paul E; Horng, Yih-Chern et al. (2002) X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation. J Am Chem Soc 124:13242-56
Guan, Jing-Qu; Vorobiev, Sergeui; Almo, Steven C et al. (2002) Mapping the G-actin binding surface of cofilin using synchrotron protein footprinting. Biochemistry 41:5765-75
Chance, Mark R; Bresnick, Anne R; Burley, Stephen K et al. (2002) Structural genomics: a pipeline for providing structures for the biologist. Protein Sci 11:723-38
Maleknia, Simin D; Kiselar, Janna G; Downard, Kevin M (2002) Hydroxyl radical probe of the surface of lysozyme by synchrotron radiolysis and mass spectrometry. Rapid Commun Mass Spectrom 16:53-61

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