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Article ; Online: Gained in translation: The power of digging deep into disease models.

Copeland, Paul R

2021 Volume 294, Issue 39, Page(s) 14201–14202

Abstract: Mutations affecting the SECISBP2 protein necessary for selenocysteine incorporation are linked to human disease, but with a wide range of clinical outcomes. To gain insight into this diversity, ... ...

Abstract	Mutations affecting the SECISBP2 protein necessary for selenocysteine incorporation are linked to human disease, but with a wide range of clinical outcomes. To gain insight into this diversity, Zhao
MeSH term(s)	Humans ; Mutation ; Protein Biosynthesis ; Selenoproteins
Chemical Substances	Selenoproteins
Language	English
Publishing date	2021-02-04
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Comment
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.H119.010864
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Article ; Online: Ribosome Fate during Decoding of UGA-Sec Codons.

Copeland, Paul R / Howard, Michael T

International journal of molecular sciences

2021 Volume 22, Issue 24

Abstract: Decoding of genetic information into polypeptides occurs during translation, generally following the codon assignment rules of the organism's genetic code. However, recoding signals in certain mRNAs can overwrite the normal rules of translation. An ... ...

Abstract	Decoding of genetic information into polypeptides occurs during translation, generally following the codon assignment rules of the organism's genetic code. However, recoding signals in certain mRNAs can overwrite the normal rules of translation. An exquisite example of this occurs during translation of selenoprotein mRNAs, wherein UGA codons are reassigned to encode for the 21st proteogenic amino acid, selenocysteine. In this review, we will examine what is known about the mechanisms of UGA recoding and discuss the fate of ribosomes that fail to incorporate selenocysteine.
MeSH term(s)	Animals ; Codon, Terminator/metabolism ; Genetic Code ; Humans ; Protein Biosynthesis ; Ribosomes/genetics ; Ribosomes/metabolism ; Selenocysteine/metabolism ; Selenoproteins/genetics ; Selenoproteins/metabolism
Chemical Substances	Codon, Terminator ; Selenoproteins ; Selenocysteine (0CH9049VIS)
Language	English
Publishing date	2021-12-08
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms222413204
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Article ; Online: The selenoprotein P 3' untranslated region is an RNA binding protein platform that fine tunes selenocysteine incorporation.

Shetty, Sumangala P / Kiledjian, Nora T / Copeland, Paul R

PloS one

2022 Volume 17, Issue 7, Page(s) e0271453

Abstract: Selenoproteins contain the 21st amino acid, selenocysteine (Sec), which is incorporated at select UGA codons when a specialized hairpin sequence, the Sec insertion sequence (SECIS) element, is present in the 3' UTR. Aside from the SECIS, selenoprotein ... ...

Abstract	Selenoproteins contain the 21st amino acid, selenocysteine (Sec), which is incorporated at select UGA codons when a specialized hairpin sequence, the Sec insertion sequence (SECIS) element, is present in the 3' UTR. Aside from the SECIS, selenoprotein mRNA 3' UTRs are not conserved between different selenoproteins within a species. In contrast, the 3'-UTR of a given selenoprotein is often conserved across species, which supports the hypothesis that cis-acting elements in the 3'-UTR other than the SECIS exert post-transcriptional control on selenoprotein expression. In order to determine the function of one such SECIS context, we chose to focus on the plasma selenoprotein, SELENOP, which is required to maintain selenium homeostasis as a selenium transport protein that contains 10 Sec residues. It is unique in that its mRNA contains two SECIS elements in the context of a highly conserved 843-nucleotide 3' UTR. Here we have used RNA affinity chromatography and identified PTBP1 as the major RNA binding protein that specifically interacts with the sequence between the two SECIS elements. We then used CRISPR/Cas9 genome editing to delete two regions surrounding the first SECIS element. We found that these sequences are involved in regulating SELENOP mRNA and protein levels, which are inversely altered as a function of selenium concentrations.
MeSH term(s)	3' Untranslated Regions/genetics ; Base Sequence ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Selenium/metabolism ; Selenocysteine/genetics ; Selenoprotein P/genetics ; Selenoprotein P/metabolism ; Selenoproteins/genetics ; Selenoproteins/metabolism
Chemical Substances	3' Untranslated Regions ; RNA, Messenger ; RNA-Binding Proteins ; Selenoprotein P ; Selenoproteins ; Selenocysteine (0CH9049VIS) ; Selenium (H6241UJ22B)
Language	English
Publishing date	2022-07-29
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0271453
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Article ; Online: The expression of essential selenoproteins during development requires SECIS-binding protein 2-like.

Kiledjian, Nora T / Shah, Rushvi / Vetick, Michael B / Copeland, Paul R

Life science alliance

2022 Volume 5, Issue 5

Abstract: The dietary requirement for selenium is based on its incorporation into selenoproteins, which contain the amino acid selenocysteine (Sec). The Sec insertion sequence (SECIS) is an RNA structure found in the 3' UTR of all selenoprotein mRNAs, and it is ... ...

Abstract	The dietary requirement for selenium is based on its incorporation into selenoproteins, which contain the amino acid selenocysteine (Sec). The Sec insertion sequence (SECIS) is an RNA structure found in the 3' UTR of all selenoprotein mRNAs, and it is required to convert in-frame UGA codons from termination to Sec-incorporating codons. SECIS-binding protein 2 (Sbp2) is required for Sec incorporation, but its paralogue, SECIS-binding protein 2-like (Secisbp2l), while conserved, has no known function. Here we determined the relative roles of Sbp2 and Secisbp2l by introducing CRISPR mutations in both genes in zebrafish. By monitoring selenoprotein synthesis with
MeSH term(s)	3' Untranslated Regions ; Animals ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Selenocysteine/genetics ; Selenocysteine/metabolism ; Selenoproteins/genetics ; Selenoproteins/metabolism ; Zebrafish/genetics
Chemical Substances	3' Untranslated Regions ; RNA-Binding Proteins ; Selenoproteins ; Selenocysteine (0CH9049VIS)
Language	English
Publishing date	2022-02-24
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202101291
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Article ; Online: New Directions for Understanding the Codon Redefinition Required for Selenocysteine Incorporation.

Howard, Michael T / Copeland, Paul R

Biological trace element research

2019 Volume 192, Issue 1, Page(s) 18–25

Abstract: The fact that selenocysteine (Sec) is delivered to the elongating ribosome by a tRNA that recognizes a UGA stop codon makes it unique and a thorn in the side of what was originally thought to be a universal genetic code. The mechanism by which this ... ...

Abstract	The fact that selenocysteine (Sec) is delivered to the elongating ribosome by a tRNA that recognizes a UGA stop codon makes it unique and a thorn in the side of what was originally thought to be a universal genetic code. The mechanism by which this redefinition occurs has been slowly coming to light over the past 30 years, but key questions remain. This review seeks to highlight the prominent mechanistic questions that will guide the direction of work in the near future. These questions arise from two major aspects of Sec incorporation: (1) novel functions for the Sec insertion sequence (SECIS) that resides in all selenoprotein mRNAs and (2) the myriad of RNA-binding proteins, both known and yet to be discovered, that act in concert to modify the translation elongation process to allow Sec incorporation.
MeSH term(s)	Animals ; Codon, Terminator ; Humans ; Peptide Chain Elongation, Translational/genetics ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Selenocysteine/genetics ; Selenocysteine/metabolism ; Selenoproteins/biosynthesis ; Selenoproteins/genetics
Chemical Substances	Codon, Terminator ; RNA-Binding Proteins ; Selenoproteins ; Selenocysteine (0CH9049VIS)
Language	English
Publishing date	2019-07-24
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	445336-0
ISSN	1559-0720 ; 0163-4984
ISSN (online)	1559-0720
ISSN	0163-4984
DOI	10.1007/s12011-019-01827-y
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Article ; Online: Ribosome Fate during Decoding of UGA-Sec Codons

Paul R. Copeland / Michael T. Howard

International Journal of Molecular Sciences, Vol 22, Iss 13204, p

2021 Volume 13204

Abstract: Decoding of genetic information into polypeptides occurs during translation, generally following the codon assignment rules of the organism’s genetic code. However, recoding signals in certain mRNAs can overwrite the normal rules of translation. An ... ...

Abstract	Decoding of genetic information into polypeptides occurs during translation, generally following the codon assignment rules of the organism’s genetic code. However, recoding signals in certain mRNAs can overwrite the normal rules of translation. An exquisite example of this occurs during translation of selenoprotein mRNAs, wherein UGA codons are reassigned to encode for the 21st proteogenic amino acid, selenocysteine. In this review, we will examine what is known about the mechanisms of UGA recoding and discuss the fate of ribosomes that fail to incorporate selenocysteine.
Keywords	selenocysteine ; selenoprotein ; SECIS ; recoding ; SECIS-binding protein ; translation termination ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Language	English
Publishing date	2021-12-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The selenoprotein P 3' untranslated region is an RNA binding protein platform that fine tunes selenocysteine incorporation.

Sumangala P Shetty / Nora T Kiledjian / Paul R Copeland

PLoS ONE, Vol 17, Iss 7, p e

2022 Volume 0271453

Abstract	Selenoproteins contain the 21st amino acid, selenocysteine (Sec), which is incorporated at select UGA codons when a specialized hairpin sequence, the Sec insertion sequence (SECIS) element, is present in the 3' UTR. Aside from the SECIS, selenoprotein mRNA 3' UTRs are not conserved between different selenoproteins within a species. In contrast, the 3'-UTR of a given selenoprotein is often conserved across species, which supports the hypothesis that cis-acting elements in the 3'-UTR other than the SECIS exert post-transcriptional control on selenoprotein expression. In order to determine the function of one such SECIS context, we chose to focus on the plasma selenoprotein, SELENOP, which is required to maintain selenium homeostasis as a selenium transport protein that contains 10 Sec residues. It is unique in that its mRNA contains two SECIS elements in the context of a highly conserved 843-nucleotide 3' UTR. Here we have used RNA affinity chromatography and identified PTBP1 as the major RNA binding protein that specifically interacts with the sequence between the two SECIS elements. We then used CRISPR/Cas9 genome editing to delete two regions surrounding the first SECIS element. We found that these sequences are involved in regulating SELENOP mRNA and protein levels, which are inversely altered as a function of selenium concentrations.
Keywords	Medicine ; R ; Science ; Q
Subject code	500
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Molecular mechanism of selenoprotein P synthesis.

Shetty, Sumangala / Copeland, Paul R

Biochimica et biophysica acta. General subjects

2018 Volume 1862, Issue 11, Page(s) 2506–2510

Abstract: Background: Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) ...

Abstract	Background: Selenoprotein synthesis requires the reinterpretation of a UGA stop codon as one that encodes selenocysteine (Sec), a process that requires a set of dedicated translation factors. Among the mammalian selenoproteins, Selenoprotein P (SELENOP) is unique as it contains a selenocysteine-rich domain that requires multiple Sec incorporation events. Scope of review: In this review we elaborate on new data and current models that provide insight into how SELENOP is made. Major conclusions: SELENOP synthesis requires a specific set of factors and conditions. General significance: As the key protein required for proper selenium distribution, SELENOP stands out as a lynchpin selenoprotein that is essential for male fertility, proper neurologic function and selenium metabolism.
Language	English
Publishing date	2018-04-12
Publishing country	Netherlands
Document type	Journal Article ; Review
ZDB-ID	60-7
ISSN	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1872-8006 ; 1879-2596 ; 1879-260X ; 1879-2642 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbagen.2018.04.011
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Article ; Online: The Selenium Transport Protein, Selenoprotein P, Requires Coding Sequence Determinants to Promote Efficient Selenocysteine Incorporation.

Shetty, Sumangala P / Copeland, Paul R

Journal of molecular biology

2018 Volume 430, Issue 24, Page(s) 5217–5232

Abstract: Selenoproteins are an essential and unique group of proteins in which selenocysteine (Sec) is incorporated in response to a stop codon (UGA). Reprograming of UGA for Sec insertion in eukaryotes requires a cis-acting stem-loop structure in the 3' ... ...

Abstract	Selenoproteins are an essential and unique group of proteins in which selenocysteine (Sec) is incorporated in response to a stop codon (UGA). Reprograming of UGA for Sec insertion in eukaryotes requires a cis-acting stem-loop structure in the 3' untranslated region of selenoprotein mRNA and several trans-acting factors. Together these factors are sufficient for Sec incorporation in vitro, but the process is highly inefficient. An additional challenge is the synthesis of selenoprotein P (SELENOP), which uniquely contains multiple UGA codons. Full-length SELENOP expression requires processive Sec incorporation, the mechanism for which is not understood. In this study, we identify core coding region sequence determinants within the SELENOP mRNA that govern SELENOP synthesis. Using
MeSH term(s)	3' Untranslated Regions ; Animals ; Codon, Terminator ; HEK293 Cells ; Humans ; Nucleic Acid Conformation ; Protein Biosynthesis ; RNA, Messenger/chemistry ; Selenocysteine/metabolism ; Selenoprotein P/chemistry ; Selenoprotein P/genetics ; Selenoprotein P/metabolism ; Selenoproteins/chemistry ; Selenoproteins/genetics ; Selenoproteins/metabolism ; Zebrafish ; Zebrafish Proteins/chemistry ; Zebrafish Proteins/genetics ; Zebrafish Proteins/metabolism
Chemical Substances	3' Untranslated Regions ; Codon, Terminator ; RNA, Messenger ; SELENOP protein, human ; Selenoprotein P ; Selenoproteins ; Zebrafish Proteins ; selenop protein, zebrafish ; Selenocysteine (0CH9049VIS)
Language	English
Publishing date	2018-09-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2018.09.005
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Article ; Online: In Vitro Translation Assays for Selenocysteine Insertion.

Pinkerton, Mark H / Copeland, Paul R

Methods in molecular biology (Clifton, N.J.)

2017 Volume 1661, Page(s) 93–101

Abstract: The molecular characterization of the protein and RNA factors that are required for Sec incorporation in mammals has been largely carried out using in vitro translation systems specifically modified for this purpose. This chapter outlines the various ... ...

Abstract	The molecular characterization of the protein and RNA factors that are required for Sec incorporation in mammals has been largely carried out using in vitro translation systems specifically modified for this purpose. This chapter outlines the various systems and modifications that have been used to decipher the mechanism of Sec incorporation.
MeSH term(s)	3' Untranslated Regions ; Animals ; Cell-Free System ; Genes, Reporter ; Protein Biosynthesis ; RNA, Messenger ; RNA, Transfer, Amino Acyl/genetics ; RNA-Binding Proteins/metabolism ; Rabbits ; Recombinant Proteins ; Reticulocytes/metabolism ; Selenocysteine/genetics ; Selenoproteins/genetics ; Selenoproteins/metabolism ; Triticum
Chemical Substances	3' Untranslated Regions ; RNA, Messenger ; RNA, Transfer, Amino Acyl ; RNA-Binding Proteins ; Recombinant Proteins ; Selenoproteins ; selenocysteinyl-tRNA ; Selenocysteine (0CH9049VIS)
Language	English
Publishing date	2017-09-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7258-6_7
Database	MEDical Literature Analysis and Retrieval System OnLINE

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