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Surface based translation: Single m...

Blanchard, Scott Christopher.

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Surface based translation: Single molecule observation of ribosome activity.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Surface based translation: Single molecule observation of ribosome activity./
Author:	Blanchard, Scott Christopher.
Description:	356 p.
Notes:	Adviser: Joseph D. Puglisi.
Contained By:	Dissertation Abstracts International63-04B.
Subject:	Biology, Cell. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3048494
ISBN:	0493628258

Surface based translation: Single molecule observation of ribosome activity.
Blanchard, Scott Christopher.

Surface based translation: Single molecule observation of ribosome activity. - 356 p.

Adviser: Joseph D. Puglisi.

Thesis (Ph.D.)--Stanford University, 2002.

The ribosome is a two subunit ribonucleoprotein particle that catalyzes protein synthesis. This process, translation, is central to expression of genetic information, is highly regulated, and is the target of multiple small molecule antibiotics. The structural and mechanistic framework for understanding ribosome function remains unclear. The goal of this thesis was to understand specific binding and positioning of tRNA substrates in the ribosome, and the subsequent movement of these substrates by the ribosomal molecular machine. A number of experimental approaches including biochemical and genetic analysis, nuclear magnetic resonance spectroscopy, and single-molecule fluorescence spectroscopy have been used. In the early portions of this thesis work, model RNA oligonucleotide domains were characterized to understand critical active sites in the ribosome. Aminoglycoside antibiotics disrupt decoding of genetic information. In chapter 2, the chemical groups in rRNA that are responsible for high-affinity drug-RNA interaction were determined. The results with this model oligonucleotide provided insights into drug mechanism and the decoding process. In chapter 3, the structure of a critical hairpin loop from the active site of the 50S subunit was solved by NMR spectroscopy. This model oligonucleotide did not mimic the function of the hairpin loop in the full RNA. The latter parts of this thesis are a response to the publication of high resolution structures of the ribosome, and the lack of dynamic information on the ribosome. In chapters 4 and 5, single-molecule fluorescence spectroscopy was applied to the ribosome. Ribosomes were immobilized on quartz surfaces and shown to be active. The dynamics of tRNA binding and passage through the ribosome was monitored using fluorescence resonance energy transfer between dye-labeled tRNAs. The results show the intrinsic dynamics of tRNA-ribosome interactions, and their dependence on ribosome state. These data show the vast potential of the single-molecule method to provide novel insights to the ribosome.

ISBN: 0493628258Subjects--Topical Terms:

1017686
Biology, Cell.

Surface based translation: Single molecule observation of ribosome activity.
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100 1 $a Blanchard, Scott Christopher. $3 1251273
245 1 0 $a Surface based translation: Single molecule observation of ribosome activity.
300 $a 356 p.
500 $a Adviser: Joseph D. Puglisi.
500 $a Source: Dissertation Abstracts International, Volume: 63-04, Section: B, page: 1746.
502 $a Thesis (Ph.D.)--Stanford University, 2002.
520 $a The ribosome is a two subunit ribonucleoprotein particle that catalyzes protein synthesis. This process, translation, is central to expression of genetic information, is highly regulated, and is the target of multiple small molecule antibiotics. The structural and mechanistic framework for understanding ribosome function remains unclear. The goal of this thesis was to understand specific binding and positioning of tRNA substrates in the ribosome, and the subsequent movement of these substrates by the ribosomal molecular machine. A number of experimental approaches including biochemical and genetic analysis, nuclear magnetic resonance spectroscopy, and single-molecule fluorescence spectroscopy have been used. In the early portions of this thesis work, model RNA oligonucleotide domains were characterized to understand critical active sites in the ribosome. Aminoglycoside antibiotics disrupt decoding of genetic information. In chapter 2, the chemical groups in rRNA that are responsible for high-affinity drug-RNA interaction were determined. The results with this model oligonucleotide provided insights into drug mechanism and the decoding process. In chapter 3, the structure of a critical hairpin loop from the active site of the 50S subunit was solved by NMR spectroscopy. This model oligonucleotide did not mimic the function of the hairpin loop in the full RNA. The latter parts of this thesis are a response to the publication of high resolution structures of the ribosome, and the lack of dynamic information on the ribosome. In chapters 4 and 5, single-molecule fluorescence spectroscopy was applied to the ribosome. Ribosomes were immobilized on quartz surfaces and shown to be active. The dynamics of tRNA binding and passage through the ribosome was monitored using fluorescence resonance energy transfer between dye-labeled tRNAs. The results show the intrinsic dynamics of tRNA-ribosome interactions, and their dependence on ribosome state. These data show the vast potential of the single-molecule method to provide novel insights to the ribosome.
590 $a School code: 0212.
650 4 $a Biology, Cell. $3 1017686
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biophysics, Medical. $3 1017681
650 4 $a Chemistry, Biochemistry. $3 1017722
650 4 $a Chemistry, Physical. $3 560527
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710 2 0 $a Stanford University. $3 754827
773 0 $t Dissertation Abstracts International $g 63-04B.
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790 1 0 $a Puglisi, Joseph D., $e advisor
791 $a Ph.D.
792 $a 2002
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3048494