Archaebacterial phenylalanyl-tRNA synthetase. Accuracy of the phenylalanyl-tRNA synthetase from the archaebacterium Methanosarcina barkeri, Zn(II)-dependent synthesis of diadenosine 5‘,5“‘-P1,P4-tetraphosphate, and immunological relationship of OFFnylalanyl-tRNA synthetases from different urkingdoms.

Rauhut, Reinhard; Gabius, Hans‐Joachim; Engelhardt, Reinhild; Cramer, Friedrich

doi:10.1016/s0021-9258(18)89712-5

Cited by 28 publications

(5 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because of these ideas, the mechanisms involved in diadenosine tetraphosphate metabolism have been actively studied. Ap4A can be synthesized in vitro by aminoacyl-tRNA synthetases, through the reaction of ATP with enzyme-bound aminoacyl adenylate (Zamecnik et al, 1966;Plateau et al, 1981;Brevet et al, 1982;Goerlich et al, 1982;Blanquet et al, 1983;Jakubowski, 1983;Led et al, 1983;Rauhut et al, 1985;Wahab & Yang, 1985;Harnett et al, 1985). In the case of some prokaryotic as well as eukaryotic aminoacyl-tRNA synthetases, these reactions are strongly stimulated by the addition of trace amounts of zinc (Plateau et al, 1981;Plateau & Blanquet, 1982; Goerlich et al, 1982;Brevet et al, 1982;Blanquet et al, 1983;Jabukowski, 1983;Goerlich & Holler, 1984;Rauhut et al, 1985).…”

mentioning

confidence: 99%

Yeast diadenosine 5',5'''-P1,P4-tetraphosphate .alpha.,.beta.-phosphorylase behaves as a dinucleoside tetraphosphate synthetase

Brevet

Coste²,

Fromant³

et al. 1987

Biochemistry

View full text Add to dashboard Cite

The diadenosine 5',5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase (Ap4A phosphorylase), recently observed in yeast [Guaranowski, A., & Blanquet, S. (1985) J. Biol. Chem. 260, 3542-3547], is shown to be capable of catalyzing the synthesis of Ap4A from ATP + ADP, i.e., the reverse reaction of the phosphorolysis of Ap4A. The synthesis of Ap4A markedly depends on the presence of a divalent cation (Ca2+, Mn2+, or Mg2+). In vitro, the equilibrium constant K = ([Ap4A][Pi])/[(ATP][ADP]) is very sensitive to pH. Ap4A synthesis is favored at low pH, in agreement with the consumption of one to two protons when ATP + ADP are converted into Ap4A and phosphate. Optimal activity is found at pH 5.9. At pH 7.0 and in the presence of Ca2+, the Vm for Ap4A synthesis is 7.4 s-1 (37 degrees C). Ap4A phosphorylase is, therefore, a valuable candidate for the production of Ap4A in vivo. Ap4A phosphorylase is also capable of producing various Np4N' molecules from NTP and N'DP. The NTP site is specific for purine ribonucleotides (N = A, G), whereas the N'DP site has a broader specificity (N' = A, C, G, U, dA). This finding suggests that the Gp4N' nucleotides, as well as the Ap4N' ones, could occur in yeast cells.

show abstract

mentioning

confidence: 99%

Yeast diadenosine 5',5'''-P1,P4-tetraphosphate .alpha.,.beta.-phosphorylase behaves as a dinucleoside tetraphosphate synthetase

Brevet

Coste²,

Fromant³

et al. 1987

Biochemistry

View full text Add to dashboard Cite

show abstract

“…As the enzymes that synthesize Ap 4 A are diverse and widespread, the specific proteins responsible for their synthesis in archaea are difficult to identify. However, it has been shown that phenylalanyl-tRNA synthetase from Methanosarcina barkeri can produce Ap 4 A (Rauhut et al 1985 ), suggesting that tRNA synthetases are a source of Ap 4 A in archaea. Whether they act as second messengers, possibly via stabilization of mRNAs via 5′ capping, remains unknown.…”

Section: Mononucleotide-based Second Messengersmentioning

confidence: 99%

Putative nucleotide-based second messengers in archaea

et al. 2023

View full text Add to dashboard Cite

Second messengers transfer signals from changing intra- and extracellular conditions to a cellular response. Over the last few decades, several nucleotide-based second messengers have been identified and characterized in especially bacteria and eukaryotes. Also in archaea, several nucleotide-based second messengers have been identified. This review will summarize our understanding of nucleotide-based second messengers in archaea. For some of the nucleotide-based second messengers, like cyclic di-AMP and cyclic oligoadenylates, their roles in archaea have become clear. Cyclic di-AMP plays a similar role in osmoregulation in euryarchaea as in bacteria, and cyclic oligoadenylates are important in the Type III CRISPR–Cas response to activate CRISPR ancillary proteins involved in antiviral defense. Other putative nucleotide-based second messengers, like 3′,5′- and 2′,3′-cyclic mononucleotides and adenine dinucleotides, have been identified in archaea, but their synthesis and degradation pathways, as well as their functions as secondary messengers, still remain to be demonstrated. In contrast, 3′-3′-cGAMP has not yet been identified in archaea, but the enzymes required to synthesize 3′-3′-cGAMP have been found in several euryarchaeotes. Finally, the widely distributed bacterial second messengers, cyclic diguanosine monophosphate and guanosine (penta-)/tetraphosphate, do not appear to be present in archaea.

show abstract

“…This series of aminoacylation with analogues reveals only quantitative differences between the plant enzymes but some qualitative differences to all previously described patterns. The property of transfer of ochratoxin A to tRNAPhe-C-C-A(3'NH2) is only shared by an archaebacterial enzyme (Rauhut et al, 1985); transfer of 2-amino-4-methylhex-4-enoic acid to tRNAPhe-C-C-A is only seen with the yeast cytoplasmic enzyme and mitochondrial enzymes from yeast and liver. In contrast to yeast, eubacterial, and archaebacterial enzymes, /V-benzyl-Dphenylalanine is not transferred.…”

Section: Resultsmentioning

confidence: 99%

“…There are, however, differences in the strategy to achieve accuracy for phenylalanyl-tRNA synthetases from a eubacterial, archaebacterial, lower (yeast, N. crassa), and higher (turkey) eukaryotic organism including their mitochondria (Gabius et al, 1983a,b;Rauhut et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

Evolutionary aspects of accuracy of phenylalanyl-tRNA synthetase. Accuracy of the cytoplasmic and chloroplastic enzymes of a higher plant (Phaseolus vulgaris)

Rauhut¹,

Gabius²,

Cramer³

1985

Biochemistry

View full text Add to dashboard Cite

The phenylalanyl-tRNA synthetases from cytoplasm and chloroplasts of bean (Phaseolus vulgaris) leaves employ different strategies with respect to accuracy. The chloroplastic enzyme that is coded for by the nuclear genome follows the pathway of posttransfer proofreading, also characteristic for enzymes from eubacteria and cytoplasm and mitochondria of lower eukaryotic organisms. In contrast, the cytoplasmic enzyme uses pretransfer proofreading in the case of noncognate natural amino acids, characteristic for higher eukaryotic organisms and archaebacteria. Dependent on the nature of the noncognate amino acid, pretransfer proofreading in this case occurs without tRNA stimulation or with tRNA stimulated with no or little effect of the nonaccepting 3'-OH group of the terminal adenosine. The fundamental mechanistic difference in proofreading between the heterotopic intracellular isoenzymes of the plant cell supports the idea of the origin of the chloroplastic gene by gene transfer from a eubacterial endosymbiont to the nucleus. Origin by duplication of the nuclear gene, as indicated for mitochondrial phenylalanyl-tRNA synthetases [Gabius, H.-J., Engelhardt, R., Schroeder, F.R., & Cramer, F. (1983) Biochemistry 22, 5306-5315], appears unlikely. Further analyses of the ATP/PPi pyrophosphate exchange and aminoacylation of tRNAPhe-C-C-A(3'NH2), using 11 phenylalanine analogues, reveal intraspecies and interspecies variability of the architecture of the amino acid binding part within the active site.

show abstract

Cited by 28 publications

References 33 publications

Yeast diadenosine 5',5'''-P1,P4-tetraphosphate .alpha.,.beta.-phosphorylase behaves as a dinucleoside tetraphosphate synthetase

Yeast diadenosine 5',5'''-P1,P4-tetraphosphate .alpha.,.beta.-phosphorylase behaves as a dinucleoside tetraphosphate synthetase

Putative nucleotide-based second messengers in archaea

Evolutionary aspects of accuracy of phenylalanyl-tRNA synthetase. Accuracy of the cytoplasmic and chloroplastic enzymes of a higher plant (Phaseolus vulgaris)

Contact Info

Product

Resources

About