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Structural and Functional Studies of Escherichia coli Ribosomes and Their Polymerization of Unnatural Monomers.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Structural and Functional Studies of Escherichia coli Ribosomes and Their Polymerization of Unnatural Monomers./
作者:	Ward, Frederick R.
出版者:	Ann Arbor : ProQuest Dissertations & Theses, : 2021,
面頁冊數:	74 p.
附註:	Source: Dissertations Abstracts International, Volume: 83-03, Section: B.
Contained By:	Dissertations Abstracts International83-03B.
標題:	Biology. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28497022
ISBN:	9798535565316

Structural and Functional Studies of Escherichia coli Ribosomes and Their Polymerization of Unnatural Monomers.
Ward, Frederick R.

Structural and Functional Studies of Escherichia coli Ribosomes and Their Polymerization of Unnatural Monomers. - Ann Arbor : ProQuest Dissertations & Theses, 2021 - 74 p.

Source: Dissertations Abstracts International, Volume: 83-03, Section: B.

Thesis (Ph.D.)--University of California, Berkeley, 2021.

This item must not be sold to any third party vendors.

The ribosome catalyzes the synthesis of polypeptides with high efficiency and sequence specificity. Repurposing the ribosome as a platform for manufacturing other sequence defined polymers could access a wide variety of previously unattainable molecules and bulk materials. In this work, we aim to understand both engineered and wild type ribosomes through structural and biochemical analysis. We reveal limitations of previous engineering efforts on the ribosome, highlighting the importance of careful mutation and selection techniques. The ribosome we study is poorly assembled and nonfunctional in vitro despite improved polymerization of β-amino acids in vivo. We identify key regions of the ribosome that are disrupted by mutations and offer suggestions for more targeted engineering that will preserve efficient ribosome assembly. We also characterize the structure of the wild type ribosome bound to an unnatural, non-α-amino acid monomer for the first time. This monomer is correctly accommodated into the P site of the ribosome, explaining previously observed activity as an initiator substrate. Lastly, we assess a new, short peptide luciferase-complementing reporter in defined in vitro translations as a better readout of mutant ribosome activity. Using this assay, we show activity of purified active site mutant ribosomes in vitro for the first time, reconciling often observed differences from in vivo systems. These projects underscore the importance of detailed characterization of both the input to and results of ambitious bioengineering efforts.

ISBN: 9798535565316Subjects--Topical Terms:

522710
Biology.
Subjects--Index Terms:

CryoEM

Structural and Functional Studies of Escherichia coli Ribosomes and Their Polymerization of Unnatural Monomers.
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245 1 0 $a Structural and Functional Studies of Escherichia coli Ribosomes and Their Polymerization of Unnatural Monomers.
260 1 $a Ann Arbor : $b ProQuest Dissertations & Theses, $c 2021
300 $a 74 p.
500 $a Source: Dissertations Abstracts International, Volume: 83-03, Section: B.
500 $a Advisor: Cate, Jamie.
502 $a Thesis (Ph.D.)--University of California, Berkeley, 2021.
506 $a This item must not be sold to any third party vendors.
520 $a The ribosome catalyzes the synthesis of polypeptides with high efficiency and sequence specificity. Repurposing the ribosome as a platform for manufacturing other sequence defined polymers could access a wide variety of previously unattainable molecules and bulk materials. In this work, we aim to understand both engineered and wild type ribosomes through structural and biochemical analysis. We reveal limitations of previous engineering efforts on the ribosome, highlighting the importance of careful mutation and selection techniques. The ribosome we study is poorly assembled and nonfunctional in vitro despite improved polymerization of β-amino acids in vivo. We identify key regions of the ribosome that are disrupted by mutations and offer suggestions for more targeted engineering that will preserve efficient ribosome assembly. We also characterize the structure of the wild type ribosome bound to an unnatural, non-α-amino acid monomer for the first time. This monomer is correctly accommodated into the P site of the ribosome, explaining previously observed activity as an initiator substrate. Lastly, we assess a new, short peptide luciferase-complementing reporter in defined in vitro translations as a better readout of mutant ribosome activity. Using this assay, we show activity of purified active site mutant ribosomes in vitro for the first time, reconciling often observed differences from in vivo systems. These projects underscore the importance of detailed characterization of both the input to and results of ambitious bioengineering efforts.
590 $a School code: 0028.
650 4 $a Biology. $3 522710
650 4 $a Protein synthesis. $3 3681687
650 4 $a Polymers. $3 535398
650 4 $a Experiments. $3 525909
650 4 $a Antibiotics. $3 670318
650 4 $a Mutation. $3 837917
650 4 $a Cloning. $3 571606
650 4 $a Optimization. $3 891104
650 4 $a Polymerization. $3 560492
650 4 $a Chemistry. $3 516420
650 4 $a Amino acids. $3 558768
650 4 $a Genomes. $3 592593
650 4 $a Engineering. $3 586835
650 4 $a E coli. $3 3556834
650 4 $a Enzymes. $3 520899
650 4 $a Polypeptides. $3 1085124
650 4 $a Transfer RNA. $3 3681688
650 4 $a Crystallography. $3 518393
650 4 $a Proteins. $3 558769
650 4 $a Molecular biology. $3 517296
650 4 $a Cellular biology. $3 3172791
653 $a CryoEM
653 $a Ribosome
653 $a Translation
653 $a Escherichia coli
653 $a Polymerization
653 $a Unnatural monomers
690 $a 0306
690 $a 0485
690 $a 0537
690 $a 0307
690 $a 0379
710 2 $a University of California, Berkeley. $b Molecular & Cell Biology. $3 2097722
773 0 $t Dissertations Abstracts International $g 83-03B.
790 $a 0028
791 $a Ph.D.
792 $a 2021
793 $a English
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28497022