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The regulation of selenoprotein tran...

Jameson, RuthAnna Reid.

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The regulation of selenoprotein translation.

Record Type:	Electronic resources : Monograph/item
Title/Author:	The regulation of selenoprotein translation./
Author:	Jameson, RuthAnna Reid.
Description:	124 p.
Notes:	Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1256.
Contained By:	Dissertation Abstracts International65-03B.
Subject:	Health Sciences, Nutrition. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3126821
ISBN:	0496740997

The regulation of selenoprotein translation.
Jameson, RuthAnna Reid.

The regulation of selenoprotein translation. - 124 p.

Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1256.

Thesis (Ph.D.)--University of Illinois at Chicago, Health Sciences Center, 2004.

The essential micronutrient selenium is biologically active through the functions of selenoproteins, into which selenium is cotranslationally incorporated as the amino acid selenocysteine in response to some in-frame UGA codons. The interpretation of UGA as selenocysteine rather than as a translation termination signal is inefficient and is dependent on specialized factors including an mRNA stem-loop, called the SECIS element, tRNA[Ser]Sec, and protein factors which bind to the SECIS element.

ISBN: 0496740997Subjects--Topical Terms:

1017801
Health Sciences, Nutrition.

The regulation of selenoprotein translation.
LDR:02710nmm 2200313 4500 001 1816609
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020 $a 0496740997
035 $a (UnM)AAI3126821
035 $a AAI3126821
040 $a UnM $c UnM
100 1 $a Jameson, RuthAnna Reid. $3 1905985
245 1 4 $a The regulation of selenoprotein translation.
300 $a 124 p.
500 $a Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1256.
500 $a Adviser: Alan M. Diamond.
502 $a Thesis (Ph.D.)--University of Illinois at Chicago, Health Sciences Center, 2004.
520 $a The essential micronutrient selenium is biologically active through the functions of selenoproteins, into which selenium is cotranslationally incorporated as the amino acid selenocysteine in response to some in-frame UGA codons. The interpretation of UGA as selenocysteine rather than as a translation termination signal is inefficient and is dependent on specialized factors including an mRNA stem-loop, called the SECIS element, tRNA[Ser]Sec, and protein factors which bind to the SECIS element.
520 $a Because the translation of UGA as selenocysteine increases with increased selenium availability, it was examined as a locus of regulation for selenoprotein levels. The regulation of UGA translation was examined using a specialized reporter construct and cell lines engineered to reflect biological effects of selenium supplementation, independent of selenium levels. The activities of selected selenoproteins, the efficiency of UGA translation, levels of tRNA [Ser]Sec and the distribution of the two tRNA[Ser]Sec isoforms were evaluated to identify conditions that contribute to the selenium induction of selenoprotein translation.
520 $a Substantial evidence was presented which indicates that one isoform of tRNA[Ser]Sec is preferentially active in the translation of UGA. It was found that factors other than the SECIS element are likely to be responsible for the differences in selenium sensitivity among selenoproteins. Furthermore, tRNA[Ser]Sec, which can be limiting for selenoprotein translation in some cellular conditions, increases in abundance in response to increased levels of selenoprotein mRNA. These results constitute new information regarding the regulation of selenoprotein translation, and suggest that it involves a complex dynamic among several factors.
590 $a School code: 0806.
650 4 $a Health Sciences, Nutrition. $3 1017801
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Biology, Cell. $3 1017686
690 $a 0570
690 $a 0307
690 $a 0379
710 2 0 $a University of Illinois at Chicago, Health Sciences Center. $3 1021703
773 0 $t Dissertation Abstracts International $g 65-03B.
790 1 0 $a Diamond, Alan M., $e advisor
790 $a 0806
791 $a Ph.D.
792 $a 2004
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3126821