The atomic resolution structure of the ?P4-P6? domain of the Tetrahymena ribozyme that was solved by Doudna and co-workers provides an intimate look at the molecular contacts that stabilize the tertiary Hstructure of an RNA. Interestingly, our studies have shown that the Hformation of the tertiary contacts that form within the P5c subdomain Hoccur slightly faster than the concerted folding of the remainder of Hthe P4-P6 domain. The P5c subdomain contains crystallographically Hdiscernible Mg2+ ions and has been postulated to be the ?trigger? for Hthe folding of the ribozyme. We are further exploring the folding Hmechanism of the Tetrahymena ribozyme by examining the folding of the Hisolated P4-P6 domain, which is seen to fold on the sub-second Htimescale in the presence of other ribozyme components. This work Halso provides the foundation for the analysis of mutations in P4-P6 Hthat enhance the rate of folding of the catalytic core, as described Hin the next subproject.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR001633-19
Application #
6491434
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
Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461
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