Literature DB >> 11568444

Evolution of selenocysteine-containing proteins: significance of identification and functional characterization of selenoproteins.

V N Gladyshev1, G V Kryukov.   

Abstract

In the genetic code, UGA serves as either a signal for termination or a codon for selenocysteine (Sec). Sec rarely occurs in protein and is different from other amino acids in that much of the biosynthetic machinery governing its incorporation into protein is unique to this amino acid. Sec-containing proteins have diverse functions and lack a common amino acid motif or consensus sequence. Sec has previously been considered to be a relic of the primordial genetic code that was counter-selected by the presence of oxygen in the atmosphere. In the present report, it is proposed that Sec was added to the already existing genetic code and its use has accumulated during evolution of eukaryotes culminating in vertebrates. The more recently evolved selenoproteins appear to take advantage of unique redox properties of Sec that are superior to those of Cys for specific biological functions. Further understanding of the evolution of selenoproteins as well as biological properties and biomedical applications of the trace element selenium requires identification and functional characterization of all mammalian selenoproteins.

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Year:  2001        PMID: 11568444     DOI: 10.1002/biof.5520140112

Source DB:  PubMed          Journal:  Biofactors        ISSN: 0951-6433            Impact factor:   6.113


  23 in total

Review 1.  How selenium has altered our understanding of the genetic code.

Authors:  Dolph L Hatfield; Vadim N Gladyshev
Journal:  Mol Cell Biol       Date:  2002-06       Impact factor: 4.272

2.  Non-animal origin of animal thioredoxin reductases: implications for selenocysteine evolution and evolution of protein function through carboxy-terminal extensions.

Authors:  Sergey V Novoselov; Vadim N Gladyshev
Journal:  Protein Sci       Date:  2003-02       Impact factor: 6.725

Review 3.  Incorporation of selenocysteine into proteins using peptide ligation.

Authors:  Robert J Hondal
Journal:  Protein Pept Lett       Date:  2005-11       Impact factor: 1.890

Review 4.  Selenium at the redox interface of the genome, metabolome and exposome.

Authors:  Jolyn Fernandes; Xin Hu; M Ryan Smith; Young-Mi Go; Dean P Jones
Journal:  Free Radic Biol Med       Date:  2018-06-05       Impact factor: 7.376

Review 5.  The molecular biology of selenocysteine.

Authors:  Jonathan N Gonzalez-Flores; Sumangala P Shetty; Aditi Dubey; Paul R Copeland
Journal:  Biomol Concepts       Date:  2013-08

Review 6.  Understanding selenoprotein function and regulation through the use of rodent models.

Authors:  Marina V Kasaikina; Dolph L Hatfield; Vadim N Gladyshev
Journal:  Biochim Biophys Acta       Date:  2012-03-13

7.  The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding.

Authors:  Christine Allmang; Philippe Carbon; Alain Krol
Journal:  RNA       Date:  2002-10       Impact factor: 4.942

8.  The microbial selenoproteome of the Sargasso Sea.

Authors:  Yan Zhang; Dmitri E Fomenko; Vadim N Gladyshev
Journal:  Genome Biol       Date:  2005-03-29       Impact factor: 13.583

Review 9.  Differing views of the role of selenium in thioredoxin reductase.

Authors:  Robert J Hondal; Erik L Ruggles
Journal:  Amino Acids       Date:  2010-02-21       Impact factor: 3.520

10.  Organic and inorganic mercurials have distinct effects on cellular thiols, metal homeostasis, and Fe-binding proteins in Escherichia coli.

Authors:  Stephen P LaVoie; Daphne T Mapolelo; Darin M Cowart; Benjamin J Polacco; Michael K Johnson; Robert A Scott; Susan M Miller; Anne O Summers
Journal:  J Biol Inorg Chem       Date:  2015-10-26       Impact factor: 3.358

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