The broad, long-term objective of the research is to obtain the structure of mammalian (rat) ribosomes and to derive from the structure a coherent molecular account of the function of the particle in protein synthesis. A requisite for the resolution of the structure is the sequences of nucleotides and of amino acids in the constituent nucleic acids and proteins. These sequences are necessary but hardly likely to be sufficient to solve the structure, just as knowledge of the structure is unlikely to lead parri passu to an understanding of the function of ribosomes. However, it is difficult to imagine being able to decipher the structure without the chemistry of the constituents or to describe function without knowledge of the structure. The chemistry may also help in understanding the evolution of ribosomes, in defining the rules that govern the interaction of the proteins and the rRNAs, and in uncovering the amino acid sequences that direct the proteins to the nucleolus for assembly on nascent rRNA. A commitment has been made both to the acquisition of the chemical data and to the solution of the structure.
The specific aims are: (1) To continue the determination of the sequences of amino acids in rat ribosomal proteins by a combination of protein chemistry and recombinant DNA technology. (2) To relate the structure of rat ribosomal proteins to their function by a combination of molecular genetic and biochemical techniques using yeast to further the aim.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
2R01GM021769-21
Application #
2173785
Study Section
Physiological Chemistry Study Section (PC)
Project Start
1975-02-01
Project End
1999-01-31
Budget Start
1995-02-01
Budget End
1996-01-31
Support Year
21
Fiscal Year
1995
Total Cost
Indirect Cost
Name
University of Chicago
Department
Biochemistry
Type
Schools of Medicine
DUNS #
225410919
City
Chicago
State
IL
Country
United States
Zip Code
60637
Rivlin, A A; Chan, Y L; Wool, I G (1999) The contribution of a zinc finger motif to the function of yeast ribosomal protein YL37a. J Mol Biol 294:909-19
Chan, Y L; Olvera, J; Wool, I G (1996) The primary structure of rat ribosomal protein L14. Biochem Biophys Res Commun 222:427-31
Chan, Y L; Olvera, J; Paz, V et al. (1996) The primary structures of rat ribosomal proteins S3a (the V-Fos transformation effector) and of S3b. Biochem Biophys Res Commun 228:141-7
Chan, Y L; Wool, I G (1996) The primary structure of rat ribosomal protein L6. Biochem Mol Biol Int 39:431-8
Olvera, J; Wool, I G (1996) The primary structure of rat ribosomal protein L10a. Biochem Biophys Res Commun 220:954-7
Chan, Y L; Diaz, J J; Denoroy, L et al. (1996) The primary structure of rat ribosomal protein L10: relationship to a Jun-binding protein and to a putative Wilms' tumor suppressor. Biochem Biophys Res Commun 225:952-6
Chan, Y L; Wool, I G (1995) The primary structure of rat ribosomal protein L22. Biochim Biophys Acta 1260:113-5
Munishkin, A; Wool, I G (1995) Systematic deletion analysis of ricin A-chain function. Single amino acid deletions. J Biol Chem 270:30581-7
Chan, Y L; Olvera, J; Wool, I G (1995) The primary structures of rat ribosomal proteins L4 and L41. Biochem Biophys Res Commun 214:810-8
Chan, Y L; Suzuki, K; Wool, I G (1995) The carboxyl extensions of two rat ubiquitin fusion proteins are ribosomal proteins S27a and L40. Biochem Biophys Res Commun 215:682-90

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