Biomaterial Database

Escherichia coli elongation factor G blocks stringent factor. 1980

E G Wagner, and C G Kurland

The relationship between the binding domains of elongation factor G(EF-G) and stringent factor (SF) on ribosomes was studied. The binding of highly purified, radioactively labeled, protein factors to ribosomes was monitored with a column system. The data show that binding of EF-G to ribosomes in the presence of fusidic acid and GDP or of the noncleavable analogue GDPCP prevents subsequent binding of SF to ribosomes. In addition, stabilization of the EF-G-ribosome complex by fusidic acid inhibits SF's enzymatic activities. Removal of protein L7/L12 from ribosomes leads to weaker binding of EF-G, while SF's binding and activity are unaffected. In the absence of L7/L12, EF-G-dependent inhibition of SF binding and function is reduced. The data presented in this report suggest that these two factors bind at overlapping, or at least interacting, ribosomal domains.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D010445	Peptide Elongation Factors	Protein factors uniquely required during the elongation phase of protein synthesis.	Elongation Factor,Elongation Factors, Peptide,Factor, Elongation,Factors, Peptide Elongation
D010770	Phosphotransferases	A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.	Kinases,Phosphotransferase,Phosphotransferases, ATP,Transphosphorylase,Transphosphorylases,Kinase,ATP Phosphotransferases
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D006150	Guanine Nucleotides		Guanine Nucleotide,Guanosine Phosphates,Nucleotide, Guanine,Nucleotides, Guanine,Phosphates, Guanosine
D006158	Guanosine Pentaphosphate	Guanosine 5'-triphosphate 2'(3')-diphosphate. A guanine nucleotide containing five phosphate groups. Three phosphate groups are esterified to the sugar moiety in the 5' position and the other two in the 2' or 3' position. This nucleotide serves as a messenger to turn off the synthesis of ribosomal RNA when amino acids are not available for protein synthesis.	(p)ppGpp,Alarmone,Alarmone pppGpp,Bacterial Magic Spot pppGpp,ppprGpp,Guanosine 3'-Diphosphate 5'-Triphosphate,3'-Diphosphate 5'-Triphosphate, Guanosine,5'-Triphosphate, Guanosine 3'-Diphosphate,Guanosine 3' Diphosphate 5' Triphosphate,Pentaphosphate, Guanosine,pppGpp, Alarmone
D006159	Guanosine Tetraphosphate	Guanosine 5'-diphosphate 2'(3')-diphosphate. A guanine nucleotide containing four phosphate groups. Two phosphate groups are esterified to the sugar moiety in the 5' position and the other two in the 2' or 3' position. This nucleotide serves as a messenger to turn off the synthesis of ribosomal RNA when amino acids are not available for protein synthesis. Synonym: magic spot I.	Alarmone ppGpp,Bacterial Magic Spot ppGpp,Guanosine 5'-(trihydrogen diphosphate), mono(trihydrogen diphosphate) (ester),Guanosine 5'-diphosphate 2'(3')-diphosphate,ppGpp,Guanosine 3'-Diphosphate 5'-Diphosphate,Guanosine 5'-Diphosphate 3'-Diphosphate,3'-Diphosphate 5'-Diphosphate, Guanosine,5'-Diphosphate 3'-Diphosphate, Guanosine,Guanosine 3' Diphosphate 5' Diphosphate,Guanosine 5' Diphosphate 3' Diphosphate,Tetraphosphate, Guanosine,ppGpp, Alarmone
D001277	GTP Pyrophosphokinase	An enzyme that catalyzes reversibly the transfer of a pyrophosphate group from ATP to the 3'-OH group of GDP or GTP with the formation of guanosine 3'-diphosphate 5'-diphosphate or guanosine 3'-diphosphate 5'-triphosphate and AMP. The enzyme, also called stringent factor, is located in the relA gene in stringent strains of bacteria. The above synthesis is induced by mRNA and uncharged tRNA which is bound to the aminoacyl-t-RNA binding site of the ribosome by a codon-specific association. EC 2.7.6.5.	ATP-Guanosine Phosphate Pyrophosphotransferase,Stringent Factor,ATP Guanosine Phosphate Pyrophosphotransferase,Factor, Stringent,Pyrophosphokinase, GTP,Pyrophosphotransferase, ATP-Guanosine Phosphate
D012270	Ribosomes	Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION.	Ribosome