Polyamine Requirement for Microbial Protein Synthesis: Structural Specificity in Cell-free Systems<i>of Escherichia coli</i>

Praisler, Rosemarie; Männlein, Elisabeth; Aschhoff, H. J.; Mach, Michael; Kersten, W.

doi:10.1515/bchm2.1984.365.2.1155

Cited by 3 publications

(1 citation statement)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, this system was equally stimulated by Spd, AP-Cad, and Hspd. Such a functional interchangeability with the structurally related triamines has been observed in the E. coli system, where conversely Nspd and AP-Cad are almost as effective as Spd (12,21). Furthermore, in polyaminedeficient mutants of E. coli, Nspd is a substitute for Spd in supporting growth (17).…”

Section: Discussionmentioning

confidence: 80%

Effect of Norspermidine and Its Related Triamines on the Cell‐Free Polyphenylalanine Synthesizing System from Vibrio parahaemolyticus

Yamamoto

Koumoto

Shikami

et al. 1990

Microbiology and Immunology

View full text Add to dashboard Cite

The effect of norspermidine and its structurally related triamines on the cell-free polyphenylalanine synthesizing system from Vibrio parahaemolyticus was examined in connection with the requirement of the system for monovalent cation . In the absence of norspermidine, the maximal incorporation of [14C] phenylalanine into hot trichloroacetic acid insoluble material was observed under ionic conditions of 12 mm Mg2+ and 50 mm NH4+. K+ could partially substitute for NH4+ , but Na+ could not. The addition of norspermidine to the polyphenylalanine synthetic reaction mixture not only lowered the optimal Mg2+ concentration , but it also stimulated the polyphenylalanine synthesis up to 2-fold with no significant increase in misincorporation of [ 14C]leucine.Other triamines having one or two methylene chains more than norspermidine were also effective in eliciting these effects . Furthermore, Na could not support the polyphenylalanine synthesis even in the presence of norspermidine and, on the contrary, inhibited the polyphenylalanine synthesis induced by NH4+ regardless of whether norspermidine was present or not . These findings are discussed in comparison with the properties of other bacterial cell-free systems.

show abstract

Section: Discussionmentioning

confidence: 80%

Effect of Norspermidine and Its Related Triamines on the Cell‐Free Polyphenylalanine Synthesizing System from Vibrio parahaemolyticus

Yamamoto

Koumoto

Shikami

et al. 1990

Microbiology and Immunology

View full text Add to dashboard Cite

show abstract

Effects of polyamine analogs on the extent and fidelity of in vitro polypeptide synthesis

Snyder¹,

Edwards²

1991

Biochemical and Biophysical Research Communications

View full text Add to dashboard Cite

Structure/function correlation of spermine‐analogue‐induced modulation of peptidyltransferase activity

Karahalios

Mamos

Karigiannis

et al. 1998

European Journal of Biochemistry

View full text Add to dashboard Cite

In a cell-free system derived from Escherichia coli,various analogues of spermine were used to study their effect on the binding of AcPhe-tRNA to poly (U)-programmed ribosomes and on the puromycin reaction carried out at 6 mM Mg 2ϩ (Ac, acetyl). In the absence of factors washable from ribosomes (FWR fraction), mono-acylated or di-acylated analogues of spermine stimulate the binding of AcPhe-tRNA to a lesser degree than spermine, in the order: N 1 -acetylspermine Ͼ N 1 ,N 12 -diacetylspermine Х N 1 ,N 12 -dipivaloylspermine. Also, the above analogues do not show any sparing effect on Mg 2ϩ requirements for AcPhe-tRNA binding to ribosomes, in contrast to spermine. The presence of FWR fraction during the binding or acetylation of the secondary amines of spermine moderates or abolishes the stimulatory effect.In addition, all analogues tested enhance the stability of the ternary complex AcPhe-tRNA-poly(U)-ribosome and the extent of AcPhe-puromycin synthesis, particularly in the absence of the FWR fraction. At the kinetic phase of AcPhe-puromycin synthesis, the analogues display both stimulatory and inhibitory effects, depending on the absence (partial noncompetitive inhibition) or the presence of the FWR fraction (nonessential activation in concert with partial noncompetitive inhibition). Detailed kinetic analysis shows that the analogues tested can mimic the behaviour of spermine, however, the potency to affect the peptidyltransferase activity depends on their degree of acylation, acyl-substituent size, charge distribution and on their chain flexibility.Keywords : acylated polyamine; protein synthesis; puromycin reaction; peptidyltransferase.Polyamines are organic polycations that are protonated at physiological pH and can potentially interact with a variety of cellular macromolecules including nucleic acids and proteins [1]. Substantial evidence exists suggesting a significant role of polyamines in regulating the translation process at several levels [1]. Due to its four positive charges, spermine is the most effective of the naturally occurring polyamines both in regulating the ribosomal functions and in decreasing the Mg 2ϩ requirements for protein synthesis. Tabor and Tabor [2] have reported that endogenous spermine does not exist in Escherichia coli. However, small amounts of spermine, about two orders of magnitude lower than those of spermidine, can be detected in E. coli by more sensitive methods [3]. Extensive biochemical studies have focused on the mechanism of spermine biological action in prokaryotic-cell-free systems, since this polyamine consists the parent compound of a large number of synthetic polyamine analogues with antiparasitic and antitumor activity [4Ϫ6].Evidently, spermine markedly stimulates the activity of several in vitro protein-synthesizing systems characterized by low Mg 2ϩ concentrations near those observed in vivo [7Ϫ10]. In a recent report [11], we have demonstrated that, at 6 mM Mg 2ϩ spermine exhibits a concentration-dependent allosteric biphasic

show abstract

Polyamine Requirement for Microbial Protein Synthesis: Structural Specificity in Cell-free Systemsof Escherichia coli

Cited by 3 publications

References 12 publications

Effect of Norspermidine and Its Related Triamines on the Cell‐Free Polyphenylalanine Synthesizing System from Vibrio parahaemolyticus

Effect of Norspermidine and Its Related Triamines on the Cell‐Free Polyphenylalanine Synthesizing System from Vibrio parahaemolyticus

Effects of polyamine analogs on the extent and fidelity of in vitro polypeptide synthesis

Structure/function correlation of spermine‐analogue‐induced modulation of peptidyltransferase activity

Contact Info

Product

Resources

About