Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli
Co-translational insertion of selenocysteine (Sec) into proteins in response to UGA codons is directed by selenocysteine insertion sequence (SECIS) elements. In known bacterial selenoprotein genes, SECIS elements are located in the coding regions immediately downstream of UGA codons. Here, we report...
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| Format: | Online |
| Language: | English |
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Oxford University Press
2005
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| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1087901/ |
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pubmed-1087901 |
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pubmed-10879012005-05-02 Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli Su, Dan Li, Yehua Gladyshev, Vadim N. Article Co-translational insertion of selenocysteine (Sec) into proteins in response to UGA codons is directed by selenocysteine insertion sequence (SECIS) elements. In known bacterial selenoprotein genes, SECIS elements are located in the coding regions immediately downstream of UGA codons. Here, we report that a distant SECIS element can also function in Sec insertion in bacteria provided that it is spatially close to the UGA codon. We expressed a mammalian phospholipid hydroperoxide glutathione peroxidase in Escherichia coli from a construct in which a natural E.coli SECIS element was located in the 3′-untranslated region (3′-UTR) and adjacent to a sequence complementary to the region downstream of the Sec UGA codon. Although the major readthrough event at the UGA codon was insertion of tryptophan, Sec was also incorporated and its insertion was dependent on the functional SECIS element in the UTR, base-pairing potential of the SECIS flanking region and the Sec UGA codon. These data provide important implications into evolution of SECIS elements and development of a system for heterologous expression of selenoproteins and show that in addition to the primary sequence arrangement between UGA codons and SECIS elements, their proximity within the tertiary structure can support Sec insertion in bacteria. Oxford University Press 2005 2005-04-29 /pmc/articles/PMC1087901/ /pubmed/15863725 http://dx.doi.org/10.1093/nar/gki547 Text en © The Author 2005. Published by Oxford University Press. All rights reserved |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Su, Dan Li, Yehua Gladyshev, Vadim N. |
| spellingShingle |
Su, Dan Li, Yehua Gladyshev, Vadim N. Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli |
| author_facet |
Su, Dan Li, Yehua Gladyshev, Vadim N. |
| author_sort |
Su, Dan |
| title |
Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli |
| title_short |
Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli |
| title_full |
Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli |
| title_fullStr |
Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli |
| title_full_unstemmed |
Selenocysteine insertion directed by the 3′-UTR SECIS element in Escherichia coli |
| title_sort |
selenocysteine insertion directed by the 3′-utr secis element in escherichia coli |
| description |
Co-translational insertion of selenocysteine (Sec) into proteins in response to UGA codons is directed by selenocysteine insertion sequence (SECIS) elements. In known bacterial selenoprotein genes, SECIS elements are located in the coding regions immediately downstream of UGA codons. Here, we report that a distant SECIS element can also function in Sec insertion in bacteria provided that it is spatially close to the UGA codon. We expressed a mammalian phospholipid hydroperoxide glutathione peroxidase in Escherichia coli from a construct in which a natural E.coli SECIS element was located in the 3′-untranslated region (3′-UTR) and adjacent to a sequence complementary to the region downstream of the Sec UGA codon. Although the major readthrough event at the UGA codon was insertion of tryptophan, Sec was also incorporated and its insertion was dependent on the functional SECIS element in the UTR, base-pairing potential of the SECIS flanking region and the Sec UGA codon. These data provide important implications into evolution of SECIS elements and development of a system for heterologous expression of selenoproteins and show that in addition to the primary sequence arrangement between UGA codons and SECIS elements, their proximity within the tertiary structure can support Sec insertion in bacteria. |
| publisher |
Oxford University Press |
| publishDate |
2005 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1087901/ |
| _version_ |
1611374251016716288 |