The ultimate expression of the genetic makeup of a cell resides in the proteins of that cell. Although protein synthesis is a complex process requiring numerous proteins and nucleicacids, to a large extent the specificity is determined by the first step of the process - the activation and transfer of an amino acid to its respective transfer RNA. Although considerable information about aminoacyl-tRNA synthetases and tRNA has been obtained, relatively little is known about the control of protein synthesis that may be exercised at the level of aminoacyl-tRNA formation. Our long term goal is the elucidation of the pathways, enzymes and regulatory factors which determine the levels of tRNA and synthetases in cells, and their effect on the various cellular processes in which aminoacyl-tRNA participates. The studies we propose should provide needed information in this central area of macromolecular metabolism.
Our specific aims are: 1) to identify, purify and determine the physiological role of nucleases involved in tRNA processing and end-turnover of tRNA; 2) to clone, sequence and obtain high level expression of the cca gene of E. coli in order to examine protein-nucleic acid interactions in the tRNA-tRNA nucleotidyltransferase system; 3) to study the structural organization of mammalian aminoacyl-tRNA synthetases with particular emphasis on the role of lipids and membranes and protein modification for formation of the high molecular weight synthetase complex; and 4) to determine how tRNA levels are regulated with regard to codon usage and to maintenance of stoichiometry with synthetases. The methods to be used will be enzymological, structural and genetic. In view of the central role of proteins in all cell functions, and the importance of aminoacyl-tRNA formation for the specificity of this process, an understanding of the mechanism and regulation of this step is of great importance. Elucidation of these aspects of protein synthesis in normal cells is a prerequisite to any understanding of abnormal situations which may occur under pathological conditions.
| Sulthana, Shaheen; Quesada, Ernesto; Deutscher, Murray P (2017) RNase II regulates RNase PH and is essential for cell survival during starvation and stationary phase. RNA 23:1456-1464 |
| Hossain, Sk Tofajjen; Deutscher, Murray P (2016) Helicase Activity Plays a Crucial Role for RNase R Function in Vivo and for RNA Metabolism. J Biol Chem 291:9438-43 |
| Liang, Wenxing; Deutscher, Murray P (2016) REP sequences: Mediators of the environmental stress response? RNA Biol 13:152-6 |
| Song, Limin; Wang, Guangyuan; Malhotra, Arun et al. (2016) Reversible acetylation on Lys501 regulates the activity of RNase II. Nucleic Acids Res 44:1979-88 |
| Chen, Hua; Dutta, Tanmay; Deutscher, Murray P (2016) Growth Phase-dependent Variation of RNase BN/Z Affects Small RNAs: REGULATION OF 6S RNA. J Biol Chem 291:26435-26442 |
| Hossain, Sk Tofajjen; Malhotra, Arun; Deutscher, Murray P (2016) How RNase R Degrades Structured RNA: ROLE OF THE HELICASE ACTIVITY AND THE S1 DOMAIN. J Biol Chem 291:7877-87 |
| Sulthana, Shaheen; Basturea, Georgeta N; Deutscher, Murray P (2016) Elucidation of pathways of ribosomal RNA degradation: an essential role for RNase E. RNA 22:1163-71 |
| Hossain, Sk Tofajjen; Malhotra, Arun; Deutscher, Murray P (2015) The Helicase Activity of Ribonuclease R Is Essential for Efficient Nuclease Activity. J Biol Chem 290:15697-706 |
| Yuan, Fenghua; Dutta, Tanmay; Wang, Ling et al. (2015) Human DNA Exonuclease TREX1 Is Also an Exoribonuclease That Acts on Single-stranded RNA. J Biol Chem 290:13344-53 |
| Liang, Wenxing; Rudd, Kenneth E; Deutscher, Murray P (2015) A role for REP sequences in regulating translation. Mol Cell 58:431-9 |
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