Author
G. Nass
Bio: G. Nass is an academic researcher from Max Planck Society. The author has contributed to research in topics: Transfer RNA & Leucyl-tRNA synthetase. The author has an hindex of 1, co-authored 1 publications receiving 27 citations.
Topics: Transfer RNA, Leucyl-tRNA synthetase
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27 citations
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TL;DR: 280 Possible Involvement of fMet-tRNAF in the Regulation of RNA Synthesis........... 280 Peptide Chain Initiation Various Organisms................................... 281 Procaryotic cells.................................... 281 Eucaryotic Cells......................................................... 281 PEPTlDE CHAIN ELONGATION............................................ 281 Elongation Factors....................................................... 281 Process of Elongations........................................................ 282 Outline of the steps in elongation
151 citations
TL;DR: Substrate-induced fluorescence variations have been used to study the association of Escherichia coli valyl-transfer RNA synthetase and its different substrates and the effect of valine upon the rate of dissociation of the enzyme-tRNA complex and the variation of fluorescence intensity induced by the binding ofValine and tRNA to this enzyme suggests that there is an interaction between the catalytic site and the tRNA binding site.
121 citations
TL;DR: In eucaryotic organisms, aminoacyl-tRNA synthetases different from those found in the cytoplasm are contained in organelles as part of their separate protein synthesizing machinery.
Abstract: Publisher Summary The aminoacyl-tRNA synthetases are a family of enzymes that play a key role in protein biosynthesis This chapter discusses the molecular and catalytic properties of aminoacyl-tRNA synthetases It also discusses the genetics and regulation of aminoacyl-tRNA synthetases In procaryotes they are contained in the nonsedimentable supernatant of cell extracts In eucaryotic organisms, aminoacyl-tRNA synthetases are found in the organelles, and in many cases these differ from the corresponding cytoplasmic enzymes The latter may not exist in a “free state” in the cytoplasm In mammalian cells, for instance, large, fast sedimenting complexes have been found, which contain some or all aminoacyl-tRNA synthetases together with tRNA or other parts of the protein synthesizing machinery The occurrence of some aminoacyl-tRNA synthetases in mammalian viruses has also recently been reported In eucaryotic organisms, aminoacyl-tRNA synthetases different from those found in the cytoplasm are contained in organelles as part of their separate protein synthesizing machinery In mitochondria, some of these enzymes are specific for mitochondrial tRNA's and will not aminoacylate tRNA from the cytoplasm of the same organism To date these enzymes are little characterized, and it is not known whether specific aminoacyl-tRNA synthetases for all 20 amino acids are present in the mitochondrion
105 citations
TL;DR: No immunological cross-reaction was detected between valyl and isoleucyl activating enzymes in spite of similarities in structure and substrate recognition, indicating the existence of one activating enzyme for valine in E. coli.
99 citations
TL;DR: Molecular weights of 18 aminoacyl-tRNA-synthetases of E. coli were estimated by gel filtration on Sephadex G-200 by determining the molecular weights of further 14 enzymes used as marker proteins for determination of the molecular weight determination.
Abstract: Molecular weights of 18 aminoacyl-tRNA-synthetases of E. coli were estimated by gel filtration on Sephadex G-200. Molecular weights calculated from S20 and D20 values are known for four of the aminoacyl-tRNA-synthetases, the phenylalanyl- (Stulberg, 1967), isoleucyl- (Baldwin and Berg, 1966), tyrosyl- (Calendar and Berg, 1966) and the arginyl-tRNA-synthetase (Stoffler and Nass, 1967). These enzymes have been used as marker proteins for determination of the molecular weights of further 14 aminoacyl-tRNA-synthetases:
The reliability of the used gel filtration for molecular weight determination is discussed.
83 citations