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By: Timothy P. O'Malley OSV Newsweekly Death is chaotic. The once vital body shuts down.... Read Catholic News Perspective

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The Rossman fold is a known RNA-binding domain in several dehydrogenases (89), and was recently shown to be important for the endoribonuclease activity of glyceraldehyde-3-phosphate dehydrogenase and two aldehyde dehydrogenases from the archaeon Sulfolobus solfataricus (90).

From: Progress in Nucleic Acid Research and Molecular Biology, 2004

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The Rossmann Fold Chromatin Protein Methyltransferases

The Rossmann fold seen in methylases has a seven-stranded core sheet, in which the first six strands are in the parallel configuration as part of the regular succession of α/β units. The topological crossover occurs between the 3rd and 4th strands, and juxtaposes the first strand (with the characteristic AdoMet-binding loop) and the 4th strand (with a key polar catalytic residue at its C-terminus) ( Fig. 1 ). However, there are variations on this basic structural template (see below). Protein methyltransferase activity appears to have arisen on multiple occasions within the Rossmann fold -containing superfamily of methylases. The most ancient of these is the HemK family of methylases that arose within the vast radiation of nucleic acid methylases with a [ND]PP[YFW] motif at the end of strand 4. Members of this family catalyze the methylation of N(5) of specific glutamines in the ribosomal protein L3 (YfcB) and the class 1 peptide release factors RF1 and RF2 (HemK). This family represents an early shift from nucleic acid- to protein-modifying activity, that appears to have occurred prior to the last universal common ancestor (LUCA) of extant life. Another ancient family that was already present in the LUCA is the PrmA family, whose representatives are seen in bacteria, archaea, and eukaryotes. While the activity of the archaeal and eukaryotic members of this family remain poorly studied, the bacterial versions catalyze the trimethylation of the NH terminus and the ɛ-amino groups of K3 and K39 of the ribosomal protein L11. Thus, it appears likely that multiple protein methylation activities were present prior to the radiation of extant organisms from the LUCA, and that these acted primarily on proteins of the translation apparatus. Eukaryotic chromatin protein methylases belong to two distinct families, namely, the PRMT and the DOT1 families. Neither of these can be traced back to the LUCA, and appear to be late innovations relative to the above families.

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Vern L Schramm , Charles Grubmeyer , in Progress in Nucleic Acid Research and Molecular Biology , 2004

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Authors: Lapyrionok, Roman V. ; Smorchkov, Andrey M.

Source: Historia , Volume 65,Number 2, January 2016, pp. 170-185(16)

Publisher: Franz Steiner Verlag

The authors analyse the key events in the course of Gracchan reforms when judicial power was transferred from triumviri agris iudicandis adsignandis to the consuls. The main objective of the paper is to define the essence of the political compromise which became the basis for this act and its consequences. In the authors' opinion judicial powers were granted to the triumviri by the lex Sempronia iudiciaria. The authors believe that in 129 BC the senate managed to repeal this law making a compromise with the Gracchans, i.e. consenting to extend the term of office of the agrarian commission.
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Keywords: AGER PUBLICUS ; AGRARKOMMISSION ; ITALIKE ; LEX SEMPRONIA AGRARIA ; SCIPIO AEMILIANUS ; TIBERIUS GRACCHUS

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Language: German

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Document Type: Research Article

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Publication date: 2016年1月1日

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