Abstract

We propose a genetic analysis of tRNA structure and function including work on synthesis and function of modified bases, and the mechanims of tRNA's role in protein synthesis and in gene regulation. Three main lines of work will be undertaken: 1. Analysis of suppressor mutations which affect tRNA sequence and base modification. Projects will include analysis of codon context effects on tRNA efficiency, new UGA suppressors and genetic analysis of the biosynthetic pathway for a modified base, the methyl ester of uridine-5-oxyacetic acid. 2. Analysis of the regulatory mechanism for the histidine operon. We will determine the DNA sequence changes for more mutants in the control (his0) region in order to refine the current model for tRNA's involvement in this mechanism. This will involve study of the derepressive effect of rif(r) and str(r) metations on operon expression. We also hope to learn how the high basal levels of operon expression are set. We will try to determine the mechansim where by the operon is subject to metabolic (ppGpp) control. The possibility of regulatory interactions between the control mechanisms for the histidine and purine pathways will be investigated. 3. Analysis of the regulatory mechanism for proline degradation. We will determine whether or not tRNA(PRO) is involved in regulation of this system and how the degradative enzyme (a bifunctional oxidase-dehydrogenase) manages to act in a regulatory capacity and also be a bifunctional, membrane-associated enzyme.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM023408-09
Application #
3271619
Study Section
(MG)
Project Start
1977-01-01
Project End
1986-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
9
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Utah
Department
Type
Schools of Arts and Sciences
DUNS #
City
Salt Lake City
State
UT
Country
United States
Zip Code
84112

  Publications

Li, Chan; Edwards, Michelle D; Jeong, Hotcherl et al. (2007) Identification of mutations that alter the gating of the Escherichia coli mechanosensitive channel protein, MscK. Mol Microbiol 64:560-74
Cornish, Rita M; Roth, John R; Poulter, C Dale (2006) Lethal mutations in the isoprenoid pathway of Salmonella enterica. J Bacteriol 188:1444-50
Grose, Julianne H; Joss, Lisa; Velick, Sidney F et al. (2006) Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress. Proc Natl Acad Sci U S A 103:7601-6
Grose, Julianne H; Bergthorsson, Ulfar; Roth, John R (2005) Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica. J Bacteriol 187:2774-82
Grose, Julianne H; Bergthorsson, Ulfar; Xu, Yaping et al. (2005) Assimilation of nicotinamide mononucleotide requires periplasmic AphA phosphatase in Salmonella enterica. J Bacteriol 187:4521-30
Cheng, W; Roth, J R (1994) Evidence for two NAD kinases in Salmonella typhimurium. J Bacteriol 176:4260-8
Xu, K; Delling, J; Elliott, T (1992) The genes required for heme synthesis in Salmonella typhimurium include those encoding alternative functions for aerobic and anaerobic coproporphyrinogen oxidation. J Bacteriol 174:3953-63
Downs, D M; Roth, J R (1991) Synthesis of thiamine in Salmonella typhimurium independent of the purF function. J Bacteriol 173:6597-604
Hughes, K T; Roth, J R; Olivera, B M (1991) A genetic characterization of the nadC gene of Salmonella typhimurium. Genetics 127:657-70
Zhu, N; Olivera, B M; Roth, J R (1989) Genetic characterization of the pnuC gene, which encodes a component of the nicotinamide mononucleotide transport system in Salmonella typhimurium. J Bacteriol 171:4402-9

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