Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck.

Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Research Abstract Details 

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Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Abstract Text:

Zoia Stoytcheva,Rosa M Tujebajeva,John W Harney,Marla J Berry,

Selenocysteine is incorporated into proteins via "recoding" of UGA from a stop codon to a sense codon, a process that requires specific secondary structures in the 3' untranslated region, termed selenocysteine incorporation sequence (SECIS) elements, and the protein factors that they recruit. Whereas most selenoprotein mRNAs contain a single UGA codon and a single SECIS element, selenoprotein P genes encode multiple UGAs and two SECIS elements. We have identified evolutionary adaptations in selenoprotein P genes that contribute to the efficiency of incorporating multiple selenocysteine residues in this protein. The first is a conserved, inefficiently decoded UGA codon in the N-terminal region, which appears to serve both as a checkpoint for the presence of factors required for selenocysteine incorporation and as a "bottleneck," slowing down the progress of elongating ribosomes. The second adaptation involves the presence of introns downstream of this inefficiently decoded UGA which confer the potential for nonsense-mediated decay when factors required for selenocysteine incorporation are limiting. Third, the two SECIS elements in selenoprotein P mRNA function with differing efficiencies, affecting both the rate and the efficiency of decoding different UGAs. The implications for how these factors contribute to the decoding of multiple selenocysteine residues are discussed.

Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Publishing Authors By Initials

Z Stoytcheva,RM Tujebajeva,JW Harney,MJ Berry,

For similar proteins: fish proteins: zebrafish proteins research abstracts see: proteins: fish proteins: zebrafish proteins research

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Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Molecular and cellular biology

VOLUME: 26

Page Numbers: 9177-84

Journal Abbreviation: Mol. Cell. Biol.

ISSN: 0270-7306

DAY: 25

MONTH: 09

YEAR: 2006

Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 8109087

Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Keywords Mesh Terms:

KEYWORDS: Zebrafish Proteins

MESH TERMS: metabolism

Chemical & Substance for Abstract: Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck. Information

Substance Name: Selenocysteine

Registry Number: 10236-58-5

Grant and Affiliation Information for Efficient incorporation of multiple selenocysteines involves an inefficient decoding step serving as a potential translational checkpoint and ribosome bottleneck.

AFFILIATION: Department of Cell and Molecular Biology, University of Hawaii at Manoa, Honolulu, HI 96813, USA.

Country: United States

AGENCY: United States NIDDK

GRANT: DK-52963

ACRONYM: DK

MEDLINETA: Mol Cell Biol

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