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Reconstitution of processive selenocysteine incorporation in wheat germ lysate provides insight into selenocysteine insertion sequence binding proteins
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TitleInfo
Title
Reconstitution of processive selenocysteine incorporation in wheat germ lysate provides insight into selenocysteine insertion sequence binding proteins
Name
(type = personal)
NamePart
(type = family)
Pinkerton
NamePart
(type = given)
Mark Hurst
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Mark Hurst Pinkerton Jr.
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author
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Brewer
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Gary
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Gary Brewer
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Advisory Committee
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chair
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Copeland
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Paul R
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Paul R Copeland
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Advisory Committee
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internal member
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(type = personal)
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(type = family)
Madura
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(type = given)
Kiran
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Kiran Madura
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Advisory Committee
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(authority = RULIB)
internal member
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(type = personal)
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(type = family)
Anthony
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(type = given)
Tracy G
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Tracy G Anthony
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Advisory Committee
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outside member
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Rutgers University
Role
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(authority = RULIB)
degree grantor
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School of Graduate Studies
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school
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Text
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theses
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2019
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2019-10
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2019
Language
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(authority = ISO 639-3:2007);
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English
Abstract
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A UGA stop codon is recoded to accommodate the incorporation of the 21st amino acid selenocysteine (Sec). For a UGA to be recoded a specialized set of cis and trans factors are required and consist of: an mRNA with an in frame UGA codon, a selenocysteine insertion sequence (SECIS) in the 3’ untranslated region (3’ UTR), a SECIS binding protein 2 (SBP2), a specific translation elongation factor (eEFSec), and a selenocysteine tRNA (Sec-tRNA[Ser]Sec). The N-terminus of SBP2 is believed to have no direct role in Sec incorporation because the C terminus of SBP2 is sufficient for the incorporation of Sec into selenoproteins that have one Sec codon. Selenoprotein P (SELENOP) is an essential selenoprotein for male fertility and proper neuron function. SELENOP is also unique in that it contains 10 selenocysteines and is involved in selenium uptake and transport. Interestingly, an in vitro translation system using wheat germ lysate, has no endogenous selenocysteine incorporation factors, cannot synthesize full length SELENOP even when all the known factors are added. The aim of this thesis is to gain insight into the mechanism of processive eukaryotic selenocysteine incorporation by in vitro reconstitution and bioinformatics.
Subject
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Topic
Biomedical Sciences
Subject
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Topic
Translation
Subject
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Topic
Selenoproteins
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Rutgers University Electronic Theses and Dissertations
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ETD_10255
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1 online resource (x, 191 pages) : illustrations
Note
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Ph.D.
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Includes bibliographical references
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School of Graduate Studies Electronic Theses and Dissertations
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rucore10001600001
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NjNbRU
Identifier
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doi:10.7282/t3-pt14-eq83
Genre
(authority = ExL-Esploro)
ETD doctoral
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Rights
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The author owns the copyright to this work.
RightsHolder
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Name
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Pinkerton
GivenName
Mark
Role
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Type
Permission or license
DateTime
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2019-09-16 16:46:17
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Name
Mark Pinkerton
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Affiliation
Rutgers University. School of Graduate Studies
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Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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Embargo
DateTime
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2019-10-31
DateTime
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2020-10-30
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after October 30th, 2020.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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