Modification of Selenoprotein mRNAs by Cap Tri-methylation

2017 ◽  
pp. 125-141 ◽  
Author(s):  
Anne-Sophie Gribling-Burrer ◽  
Gilbert Eriani ◽  
Christine Allmang
Keyword(s):  
Selenoprotein Mrnas

scholarly journals Efficient Incorporation of Multiple Selenocysteines Involves an Inefficient Decoding Step Serving as a Potential Translational Checkpoint and RibosomeBottleneck

2006 ◽  
Vol 26 (24) ◽  
pp. 9177-9184 ◽  
Author(s):  
Zoia Stoytcheva ◽  
Rosa M. Tujebajeva ◽  
John W. Harney ◽  
Marla J. Berry
Keyword(s):  
Untranslated Region ◽  
Stop Codon ◽  
Secondary Structures ◽  
Selenoprotein P ◽  
Secis Element ◽  
Nonsense Mediated Decay ◽  
Slowing Down ◽  
Uga Codon ◽  
Sense Codon ◽  
Selenoprotein Mrnas

ABSTRACT 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.

scholarly journals A Protein Binds the Selenocysteine Insertion Element in the 3'-UTR of Mammalian Selenoprotein mRNAs

1996 ◽  
Vol 24 (3) ◽  
pp. 464-469 ◽  
Author(s):  
N. Hubert ◽  
R. Walczak ◽  
P. Carbon ◽  
A. Krol
Keyword(s):  
Insertion Element ◽  
Selenoprotein Mrnas

scholarly journals Selenium-Related Transcriptional Regulation of Gene Expression

2018 ◽  
Author(s):  
Mikko J. Lammi ◽  
Chengjuan Qu
Keyword(s):  
Stop Codon ◽  
Regulation Of Gene Expression ◽  
Selenium Deficiency ◽  
Mrna Levels ◽  
Translation Elongation ◽  
Nonsense Mediated Decay ◽  
Specific Complex ◽  
System Functioning ◽  
The One ◽  
Selenoprotein Mrnas

Selenium is a trace metal essential to human health, and its deficiency has been related to, for instance, cardiovascular and myodegenerative diseases, infertility and osteochondropathy Kashin-Beck disease. It is incorporated as selenocysteine to selenoproteins, which protect against reactive oxygen and nitrogen species. They also participate in the activation of thyroid hormone, and play a role in immune system functioning. The synthesis and incorporation of selenocysteine occurs via a special mechanism, which differs from the one used for standard amino acids. The codon for selenocysteine is the regular in-frame stop codon, which can be passed by specific complex machinery participating in translation elongation and termination. This includes the presence of selenocysteine insertion sequence (SECIS) in the 3’-untranslated part of the selenoprotein mRNAs. Selenium deficiency is known to control both selenoprotein and non-selenoprotein transcriptomes. Nonsense-mediated decay is involved in the regulation of selenoprotein mRNA levels, both other mechanisms are also possible.

scholarly journals New insights into how selenoprotein mRNAs elude nonsense mediated decay

2006 ◽  
Vol 20 (5) ◽  
Author(s):  
Marla J Berry ◽  
Peter Hoffmann ◽  
Andrea Small‐Howard ◽  
Lucia Jesus ◽  
Erin Forry ◽  
...  
Keyword(s):  
Nonsense Mediated Decay ◽  
Selenoprotein Mrnas

Differential regulation of rat liver selenoprotein mRNAs in selenium deficiency

1992 ◽  
Vol 185 (1) ◽  
pp. 260-263 ◽  
Author(s):  
Kristina E. Hill ◽  
P. Reid Lyons ◽  
Raymond F. Burk
Keyword(s):  
Rat Liver ◽  
Selenium Deficiency ◽  
Differential Regulation ◽  
Selenoprotein Mrnas

scholarly journals Hypermethylated-capped selenoprotein mRNAs in mammals

2014 ◽  
Vol 42 (13) ◽  
pp. 8663-8677 ◽  
Author(s):  
Laurence Wurth ◽  
Anne-Sophie Gribling-Burrer ◽  
Céline Verheggen ◽  
Michael Leichter ◽  
Akiko Takeuchi ◽  
...  
Keyword(s):  
Selenoprotein Mrnas

scholarly journals The Interaction between Dietary Selenium Intake and Genetics in Determining Cancer Risk and Outcome

Nutrients ◽  
2020 ◽  
Vol 12 (8) ◽  
pp. 2424 ◽  
Author(s):  
Shrinidhi Kadkol ◽  
Alan M. Diamond
Keyword(s):  
Protein Synthesis ◽  
Cancer Risk ◽  
Cancer Progression ◽  
Disease Risk ◽  
Regulatory Element ◽  
Epidemiological Studies ◽  
Uga Codon ◽  
Dietary Component ◽  
Allelic Variations ◽  
Selenoprotein Mrnas

There is considerable interest in the trace element selenium as a possible cancer chemopreventive dietary component, but supplementation trials have not indicated a clear benefit. Selenium is a critical component of selenium-containing proteins, or selenoproteins. Members of this protein family contain selenium in the form of selenocysteine. Selenocysteine is encoded by an in-frame UGA codon recognized as a selenocysteine codon by a regulatory element, the selenocysteine insertion sequence (SECIS), in the 3′-untranslated region of selenoprotein mRNAs. Epidemiological studies have implicated several selenoprotein genes in cancer risk or outcome based on associations between allelic variations and disease risk or mortality. These polymorphisms can be found in or near the SECIS or in the selenoprotein coding sequence. These variations both function to control protein synthesis and impact the efficiency of protein synthesis in response to the levels of available selenium. Thus, an individual’s genetic makeup and nutritional intake of selenium may interact to predispose them to acquiring cancer or affect cancer progression to lethality.

scholarly journals Nucleolin binds to a subset of selenoprotein mRNAs and regulates their expression

2011 ◽  
Vol 39 (15) ◽  
pp. 6844-6844
Author(s):  
A. C. Miniard ◽  
L. M. Middleton ◽  
M. E. Budiman ◽  
C. A. Gerber ◽  
D. M. Driscoll
Keyword(s):  
Selenoprotein Mrnas
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