By Vadim N. Gladyshev, Dolph L. Hatfield (auth.), John F. Atkins, Raymond F. Gesteland (eds.)

The dynamic nature of deciphering the data in messenger RNA used to be unanticipated on the time the genetic code used to be first deciphered. We now recognize that either the which means of person codons and the framing of the readout approach should be changed by means of details in particular messenger RNAs. This ebook describes this "Recoding" phenomenon, revealing the variety of an extra layer of data in mRNAs that serves to complement the expression of genes. wisdom of recoding is key for realizing the association and expression of genes in viruses and all organisms starting from micro organism to archeae to vegetation to people, making Recoding pertinent to all organic sciences.

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Trends Genet 22:357–360 Lobanov AV, Delgado C, Rahlfs S, Novoselov SV, Kryukov GV, Gromer S, Hatfield DL, Becker K, Gladyshev VN (2006b) The plasmodium selenoproteome. Nucl Acids Res 34: 496–505 Lobanov AV, Gromer S, Salinas G, Gladyshev VN (2006c) Selenium metabolism in Trypanosoma: characterization of selenoproteomes and identification of a Kinetoplastida-specific selenoprotein. Nucleic Acids Res 34:4012–4024 Lobanov AV, Fomenko DE, Zhang Y, Sengupta A, Hatfield DL, Gladyshev VN (2007) Evolutionary dynamics of eukaryotic selenoproteomes: large selenoproteomes may associate with aquatic and small with terrestrial life.

A) The bacterial selenocysteine elongation factor (green) binds the Sec-tRNA and also binds directly to the bacterial SECIS element (red) located adjacent to and downstream of the UGA codon to deliver the Sec-tRNA to the ribosome. (B) Similarly, the archaeal elongation factor binds to the Sec-tRNA and interacts with the 3 UTR SECIS element analogous to the situation in eukaryotes. (C) In eukaryotes the SECIS element binds to SBP2 (orange) which binds to Sec-tRNA-bound EFsec. SBP2 also binds to the ribosome.

Two additional proteins previously known for other functions were identified as components of the selenocysteine incorporation machinery. , 2000). These factors and their roles in selenocysteine insertion are discussed in more detail below (see Fig. 1C). Finally, recent studies have shed light on the roles of two additional factors that had been implicated in the selenoprotein biosynthesis pathway. , 1992). Both proteins were shown to bind Sec-tRNA[Ser]Sec .

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