We are analyzing https://link.springer.com/article/10.1007/s00018-005-5402-y.

Title:
Size matters: a view of selenocysteine incorporation from the ribosome | Cellular and Molecular Life Sciences
Description:
This review focuses on the known factors required for selenocysteine (Sec) incorporation in eukaryotes and highlights recent findings that have compelled us to propose a new model for the mechanism of Sec incorporation. In light of this data we also review the controversial aspects of the previous modelspecifically regarding the proposed interaction between SBP2 and eEFSec. In addition, the relevance of two recently discovered factors in the recoding of Sec are reviewed. The role of the ribosome in this process is emphasized along with a detailed analysis of kinkturn structures present in the ribosome and the L7Ae RNA-binding motif present in SBP2 and other proteins.
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Keywords {🔍}

sbp, secis, element, sec, ribosome, article, incorporation, google, scholar, binding, cas, pubmed, interaction, motif, eefsec, protein, rna, selenocysteine, factors, function, proteins, structure, translation, uga, factor, rpl, selenoprotein, data, copeland, ribosomal, model, lae, domain, kinkturn, rnabinding, recoding, eukaryotic, codon, elements, interact, fact, insertion, bind, required, found, acids, ribosomes, secisbinding, rrna, shown,

Topics {✒️}

eefsec/sec-trna[ser]sec complex eefsec/sec-trna[ser]sec binding accommodates eefsec/sectrna[ser]sec allowing sec-trna[ser]sec eefsec/sec-trna[ser]sec article download pdf specific rna/protein contacts 5-kda snrna-binding protein sec-trna[ser]sec sec-trna[ser]sec [12] sec-specific elongation factor large salt-sensitive complex eukaryotic c-terminal extensions canonical rna-binding domain 32p-labeled secis element consensus kink-turn motif l7ae rna-binding motif c-terminal extension relative l7ae rna-binding domain ribosomal kink-turn motifs tag-tag interaction resulting wild-type secis element ribosomal protein l30 cold spring harbor secis-binding protein sbp2 full size image ribosome-binding domains overlap kink-turn rna structure archaeon methanococcus jannaschii u4 snrna fragment privacy choices/manage cookies ga base pairing uga-selenocysteine recoding machinery protein synthesis field secis element-dependent specificity truncation analysis reveals large ribosomal subunit a-site conformation change sbp2 secis-binding domain elongation factor awaits mammalian elongation factor secis-binding protein secis-binding protein-2 secis-binding protein 2 c-terminal extension cis-acting factors required rna structural motif base pairs distinct ribosomal a-site ribosomal binding site

Questions {❓}

(1994) A novel RNA-binding motif in omnipotent suppressors of translation termination, ribosomal proteins and a ribosome modification enzyme?
(2003) Termination of translation: interplay of mRNA, rRNAs and release factors?
(2004) How strong is the case for regulation of the initiation step of translation by elements at the 3′ end of eukaryotic mRNAs?

Schema {🗺️}

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         headline:Size matters: a view of selenocysteine incorporation from the ribosome
         description:This review focuses on the known factors required for selenocysteine (Sec) incorporation in eukaryotes and highlights recent findings that have compelled us to propose a new model for the mechanism of Sec incorporation. In light of this data we also review the controversial aspects of the previous modelspecifically regarding the proposed interaction between SBP2 and eEFSec. In addition, the relevance of two recently discovered factors in the recoding of Sec are reviewed. The role of the ribosome in this process is emphasized along with a detailed analysis of kinkturn structures present in the ribosome and the L7Ae RNA-binding motif present in SBP2 and other proteins.
         datePublished:2005-12-27T00:00:00Z
         dateModified:2005-12-27T00:00:00Z
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      headline:Size matters: a view of selenocysteine incorporation from the ribosome
      description:This review focuses on the known factors required for selenocysteine (Sec) incorporation in eukaryotes and highlights recent findings that have compelled us to propose a new model for the mechanism of Sec incorporation. In light of this data we also review the controversial aspects of the previous modelspecifically regarding the proposed interaction between SBP2 and eEFSec. In addition, the relevance of two recently discovered factors in the recoding of Sec are reviewed. The role of the ribosome in this process is emphasized along with a detailed analysis of kinkturn structures present in the ribosome and the L7Ae RNA-binding motif present in SBP2 and other proteins.
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         eEFSec
         L7Ae
         L30
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
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