Pyridine-promoted factor- and energy-free peptide synthesis systems prepared from various organisms including prokaryote, eukaryote, and mitochondria

Takahiko Nojima, Itaru Nitta, Takuya Ueda, Kimitsuna Watanabe

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

We demonstrate here that ribosomes from not only Escherichia coli and Thermus thermophilus but also yeast and bovine mitochondria catalyze peptide synthesis promoted by a high concentration of pyridine in the absence of soluble protein factors and chemical energy sources, and compare some characteristic features of the reactions among these organisms. Sensitivities against antibiotics, chloramphenicol and cycloheximide, showed the same tendency to those in the in vitro aqueous translation systems of these organisms, suggesting that the basic mechanism for peptide synthesis is the same among these organisms. The optimal concentration of pyridine was centered at 50% for all systems, although the dependencies on the pyridine concentrations and the yields of the products were different from one another. All these systems required Mg2+, and only mitochondrial system showed the extra Mn2+-requirement, which enhanced the yield by several fold. The optimum reaction temperatures coincided closely with the growing temperatures of the organisms except for the mitochondrial system, which showed the highest activity above 80°C. The rationale for these observations remains to be solved.

Original languageEnglish
Pages (from-to)1076-1079
Number of pages4
JournalJournal of biochemistry
Volume119
Issue number6
DOIs
Publication statusPublished - 1996 Jan 1
Externally publishedYes

Fingerprint

Mitochondria
Eukaryota
Free energy
Peptides
Thermus thermophilus
Temperature
Chloramphenicol
Cycloheximide
Ribosomes
Yeast
Escherichia coli
Yeasts
Anti-Bacterial Agents
pyridine
Proteins

Keywords

  • Antibiotics
  • Mn ion
  • Peptide synthesis system
  • Pyridine
  • Ribosomes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Pyridine-promoted factor- and energy-free peptide synthesis systems prepared from various organisms including prokaryote, eukaryote, and mitochondria. / Nojima, Takahiko; Nitta, Itaru; Ueda, Takuya; Watanabe, Kimitsuna.

In: Journal of biochemistry, Vol. 119, No. 6, 01.01.1996, p. 1076-1079.

Research output: Contribution to journalArticle

Nojima, Takahiko ; Nitta, Itaru ; Ueda, Takuya ; Watanabe, Kimitsuna. / Pyridine-promoted factor- and energy-free peptide synthesis systems prepared from various organisms including prokaryote, eukaryote, and mitochondria. In: Journal of biochemistry. 1996 ; Vol. 119, No. 6. pp. 1076-1079.
@article{af1569d02eb74017995906b3192c36d0,
title = "Pyridine-promoted factor- and energy-free peptide synthesis systems prepared from various organisms including prokaryote, eukaryote, and mitochondria",
abstract = "We demonstrate here that ribosomes from not only Escherichia coli and Thermus thermophilus but also yeast and bovine mitochondria catalyze peptide synthesis promoted by a high concentration of pyridine in the absence of soluble protein factors and chemical energy sources, and compare some characteristic features of the reactions among these organisms. Sensitivities against antibiotics, chloramphenicol and cycloheximide, showed the same tendency to those in the in vitro aqueous translation systems of these organisms, suggesting that the basic mechanism for peptide synthesis is the same among these organisms. The optimal concentration of pyridine was centered at 50{\%} for all systems, although the dependencies on the pyridine concentrations and the yields of the products were different from one another. All these systems required Mg2+, and only mitochondrial system showed the extra Mn2+-requirement, which enhanced the yield by several fold. The optimum reaction temperatures coincided closely with the growing temperatures of the organisms except for the mitochondrial system, which showed the highest activity above 80°C. The rationale for these observations remains to be solved.",
keywords = "Antibiotics, Mn ion, Peptide synthesis system, Pyridine, Ribosomes",
author = "Takahiko Nojima and Itaru Nitta and Takuya Ueda and Kimitsuna Watanabe",
year = "1996",
month = "1",
day = "1",
doi = "10.1093/oxfordjournals.jbchem.a021350",
language = "English",
volume = "119",
pages = "1076--1079",
journal = "Journal of Biochemistry",
issn = "0021-924X",
publisher = "Oxford University Press",
number = "6",

}

TY - JOUR

T1 - Pyridine-promoted factor- and energy-free peptide synthesis systems prepared from various organisms including prokaryote, eukaryote, and mitochondria

AU - Nojima, Takahiko

AU - Nitta, Itaru

AU - Ueda, Takuya

AU - Watanabe, Kimitsuna

PY - 1996/1/1

Y1 - 1996/1/1

N2 - We demonstrate here that ribosomes from not only Escherichia coli and Thermus thermophilus but also yeast and bovine mitochondria catalyze peptide synthesis promoted by a high concentration of pyridine in the absence of soluble protein factors and chemical energy sources, and compare some characteristic features of the reactions among these organisms. Sensitivities against antibiotics, chloramphenicol and cycloheximide, showed the same tendency to those in the in vitro aqueous translation systems of these organisms, suggesting that the basic mechanism for peptide synthesis is the same among these organisms. The optimal concentration of pyridine was centered at 50% for all systems, although the dependencies on the pyridine concentrations and the yields of the products were different from one another. All these systems required Mg2+, and only mitochondrial system showed the extra Mn2+-requirement, which enhanced the yield by several fold. The optimum reaction temperatures coincided closely with the growing temperatures of the organisms except for the mitochondrial system, which showed the highest activity above 80°C. The rationale for these observations remains to be solved.

AB - We demonstrate here that ribosomes from not only Escherichia coli and Thermus thermophilus but also yeast and bovine mitochondria catalyze peptide synthesis promoted by a high concentration of pyridine in the absence of soluble protein factors and chemical energy sources, and compare some characteristic features of the reactions among these organisms. Sensitivities against antibiotics, chloramphenicol and cycloheximide, showed the same tendency to those in the in vitro aqueous translation systems of these organisms, suggesting that the basic mechanism for peptide synthesis is the same among these organisms. The optimal concentration of pyridine was centered at 50% for all systems, although the dependencies on the pyridine concentrations and the yields of the products were different from one another. All these systems required Mg2+, and only mitochondrial system showed the extra Mn2+-requirement, which enhanced the yield by several fold. The optimum reaction temperatures coincided closely with the growing temperatures of the organisms except for the mitochondrial system, which showed the highest activity above 80°C. The rationale for these observations remains to be solved.

KW - Antibiotics

KW - Mn ion

KW - Peptide synthesis system

KW - Pyridine

KW - Ribosomes

UR - http://www.scopus.com/inward/record.url?scp=0029944131&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029944131&partnerID=8YFLogxK

U2 - 10.1093/oxfordjournals.jbchem.a021350

DO - 10.1093/oxfordjournals.jbchem.a021350

M3 - Article

C2 - 8827440

AN - SCOPUS:0029944131

VL - 119

SP - 1076

EP - 1079

JO - Journal of Biochemistry

JF - Journal of Biochemistry

SN - 0021-924X

IS - 6

ER -