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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Caban, Kelvin Donovan, Jesse Ranaweera, Ruchira Copeland, Paul R. Gonzalez-flores, Jonathan N. |
| Description | Author Affiliation: Donovan J ( Department of Molecular Genetics, Microbiology and Immunology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.) |
| Abstract | Selenocysteine (Sec) is incorporated at UGA codons in mRNAs possessing a Sec insertion sequence (SECIS) element in their 3'-untranslated region. At least three additional factors are necessary for Sec incorporation: SECIS-binding protein 2 (SBP2), Sec-tRNA(Sec), and a Sec-specific translation elongation factor (eEFSec). The C-terminal half of SBP2 is sufficient to promote Sec incorporation in vitro, which is carried out by the concerted action of a novel Sec incorporation domain and an L7Ae RNA-binding domain. Using alanine scanning mutagenesis, we show that two distinct regions of the Sec incorporation domain are required for Sec incorporation. Physical separation of the Sec incorporation and RNA-binding domains revealed that they are able to function in trans and established a novel role of the Sec incorporation domain in promoting SECIS and eEFSec binding to the SBP2 RNA-binding domain. We propose a model in which SECIS binding induces a conformational change in SBP2 that recruits eEFSec, which in concert with the Sec incorporation domain gains access to the ribosomal A site. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 50 |
| Volume Number | 283 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2008-12-12 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Peptide Elongation Factors Chemistry RNA-Binding Proteins Selenocysteine 3' Untranslated Regions Alanine Amino Acid Sequence Molecular Sequence Data Mutagenesis Mutation Metabolism Protein Binding Protein Structure, Tertiary Recombinant Proteins Ribosomes Sequence Homology, Amino Acid Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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