Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction.

Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction. Research Abstract Details 

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Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction. Abstract Text:

M Kawakita,K Arai,Y Kaziro,

Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction. Publishing Authors By Initials

M Kawakita,K Arai,Y Kaziro,

For similar investigative techniques: centrifugation: ultracentrifugation research abstracts see: investigative techniques: centrifugation: ultracentrifugation research

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Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 76

Page Numbers: 801-9

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Oct

YEAR: 1974

Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction. Keywords Mesh Terms:

KEYWORDS: Ultracentrifugation

MESH TERMS: metabolism

Chemical & Substance for Abstract: Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction. Information

Substance Name: Phosphoric Diester Hydrolases

Registry Number: EC 3.1.4.-

Grant and Affiliation Information for Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction.

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Country: JAPAN

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MEDLINETA: J Biochem

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Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction Related Publications

• A new extragenic suppressor of cya mutation. Mutant cyclic AMP receptor protein with an increased affinity for cyclic AMP.
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• Binding of aminoacyl-tRNA to ribosomes promoted by elongation factor Tu. Studies on the role of GTP hydrolysis.
• Conformational transition of polypeptide chain elongation factor G as determined by electron spin resonance.
• Conformational transitions of polypeptide chain elongation factor Tu. I. Studies with hydrophobic probes.
• Conformational transitioons of polypeptide chain elongation factor Tu. II. Further studies by electron spin resonance.
• Coordination of levels of elongation factors Tu, Ts, and G, and ribosomal protein SI in Escherichia coli.
• Distribution of the low molecular weight form of eukaryotic elongation factor 1 in various tissues.
• Formation of a binary complex between elongation factor G and guanine nucleotides.
• Further studies on the interaction of the polypeptide chain elongation factor G with guanine nucleotides.
• Further studies on the properties of the polypeptide chain elongation factors Tu and Ts: hydrogen-tritium exchange, optical rotatory dispersion, and intrinsic fluorescence.
• Interactions between elongation factor tu-guanosine triphosphate and ribosomes and the role of ribosome-bound transfer RNA in guanosine triphosphatase reaction.
• Involvement of 30S ribosomal protein S1 in poly(U)-directed polyphenylalanine synthesis.
• Limited hydrolysis of the polypeptide chain elongation factor Tu by trypsin. Isolation and characterization of the polypeptide fragments.
• Mechanism of action of chromomycin A3. 1. Inhibition of nucleic acid metabolism in Bacillus subtilis cells.
• Mechanism of the ribosome-dependent uncoupled GTPase reaction catalyzed by polypeptide chain elongation factor G.
• Proceedings: Polypeptide chain elongation in bacterial and mammalian systems.
• Properties and function of the sulfhydryl group in the polypeptide chain elongation factor G from E. coli.
• Purification and properties of polypeptide chain elongation factor-1 beta gamma from pig liver.
• Purification and properties of polypeptide chain elongation factor-1alpha from pig liver.
• Purification and properties of the polypeptide chain release factor (RF-4) from an extreme thermophile, Thermus thermophilus HB8.
• Purification of tubulin from bovine brain and its interaction with guanine nucleotides.
• Role of GTP in the assembly of microtubules.
• Studies on amino-acyl-sRNA synthetases from Pseudomonas and methionyl-sRNA. I. Partial purification of leucyl-, phenylalanyl-, tyrosyl-, and synthetases.
• Studies on polypeptide elongation factor 2 from pig liver. I. Purification and properties.
• Studies on polypeptide elongation factor 2 from pig liver. III. Interaction with guanine nucleotides in the presence and absence of ribosomes.
• Studies on the polypeptide elongation factors form E. coli. VI. Characterization of sulfhydryl groups in EF-Tu and EF-Ts.
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• Studies on the polypeptide elongation factors from E. coli. V. Properties of various complexes containing EF-Tu and EF-Ts.
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