2026-09-19T11:43:10Zhttps://dspace.mit.edu/server/oai/requestoai:dspace.mit.edu:1721.1/973732026-06-16T18:14:46Zcom_1721.1_7582com_1721.1_7581col_1721.1_131022
Hidde Ploegh.
Damon, Jadyn Rose
Massachusetts Institute of Technology. Department of Biology.
Massachusetts Institute of Technology. Department of Biology
2015-06-10T19:15:01Z
2015-06-10T19:15:01Z
2015
2015
http://hdl.handle.net/1721.1/97373
910734109
Thesis: Ph. D., Massachusetts Institute of Technology, Department of Biology, 2015.
Cataloged from PDF version of thesis.
Includes bibliographical references.
Ubiquitin and ubiquitin-like proteins (UBLs) have a diverse array of functions that serve to regulate many cellular processes in eukaryotic cells. The ubiquitin-related modifier UrmI is a conserved UBL that, in addition to serving as a protein modifier, functions as a sulfur carrier in tRNA thiolation reactions. Urml is required for formation of the s2 moiety that is found as part of the more complex mcm5 s2 U34 modification on the anticodon wobble uridines of tGliUUC, of tGgluUUG and tLysUUU tRNAs in a variety of organisms. It has become increasingly clear that tRNA modifications serve to alter the properties of tRNA molecules, and that tRNA modifications can impact the translational regulation of gene expression, but how specific modifications are connected to cellular processes remains largely unknown. This work focuses on Urml-dependent tRNA modifications in Saccharomyces cerevisiae. This thesis describes the phenotypes of URM] pathway mutants, and describes the physiological consequences in cells that lack the ability to thiolate tRNAs: slow growth, impaired translation and the increased activation of at least one stress response pathway. This thesis also describes a condition, growth at 37°C, that results in a decrease in tRNA thiolation in wild type cells. This decrease in tRNA thiolation requires the activity of RNA polymerase III and is accompanied by decreased levels of proteins that are involved in the tRNA thiolation pathway. This decrease in tRNA thiolation may be an adaptive strategy used by cells under specific growth conditions, and is an example of the condition specific modulation of tRNA modification levels
by Jadyn Rose Damon.
Ph.D.
174 pages in various pagings
eng
Massachusetts Institute of Technology
M.I.T. theses are protected by copyright. They may be viewed from this source for any purpose, but reproduction or distribution in any format is prohibited without written permission. See provided URL for inquiries about permission.
http://dspace.mit.edu/handle/1721.1/7582
Biology.
The physiological consequences of loss of tRNA thiolation in Saccharomyces cerevisiae
Physiological consequences of loss of transfer ribonucleic acid thiolation in Saccharomyces cerevisiae
Thesis
application/pdf
Publication
unknown
unknown
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<Abstract>Ubiquitin and ubiquitin-like proteins (UBLs) have a diverse array of functions that serve to regulate many cellular processes in eukaryotic cells. The ubiquitin-related modifier UrmI is a conserved UBL that, in addition to serving as a protein modifier, functions as a sulfur carrier in tRNA thiolation reactions. Urml is required for formation of the s2 moiety that is found as part of the more complex mcm5 s2 U34 modification on the anticodon wobble uridines of tGliUUC, of tGgluUUG and tLysUUU tRNAs in a variety of organisms. It has become increasingly clear that tRNA modifications serve to alter the properties of tRNA molecules, and that tRNA modifications can impact the translational regulation of gene expression, but how specific modifications are connected to cellular processes remains largely unknown. This work focuses on Urml-dependent tRNA modifications in Saccharomyces cerevisiae. This thesis describes the phenotypes of URM] pathway mutants, and describes the physiological consequences in cells that lack the ability to thiolate tRNAs: slow growth, impaired translation and the increased activation of at least one stress response pathway. This thesis also describes a condition, growth at 37°C, that results in a decrease in tRNA thiolation in wild type cells. This decrease in tRNA thiolation requires the activity of RNA polymerase III and is accompanied by decreased levels of proteins that are involved in the tRNA thiolation pathway. This decrease in tRNA thiolation may be an adaptive strategy used by cells under specific growth conditions, and is an example of the condition specific modulation of tRNA modification levels</Abstract>
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