Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation.

Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation. Research Abstract Details 

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Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation. Abstract Text:

K Ogata,R Ohno,K Terao,K Iwasaki,Y Endo,

The properties and role in peptide elongation of ATPase intrinsic to rat liver ribosomes were investigated. (i) Rat liver 80S ribosomes showed high ATPase and GTPase activities, whereas the GTPase activity of EF-1alpha and EF-2 was very low. mRNA, aminoacyl-tRNA, and elongation factors alone enhanced ribosomal ATPase activity and in combination stimulated it additively or synergistically. The results suggest that these translational components induce positive conformational changes of 80S ribosomes by binding to different regions of ribosomes. Translation inhibitors, tetracyclin and fusidic acid, inhibited ribosomal ATPase with or without elongational components. (ii) Two ATPase inhibitors, AMP-P(NH)P and vanadate, did not inhibit GTPase activities of EF-1alpha and EF-2 assayed as uncoupled GTPase, but they did inhibit poly(U)-dependent polyphe synthesis of 80S ribosomes. (iii) Effects of AMP-P(NH)P and ATP on poly(U)-dependent polyphe synthesis at various concentrations of GTP were examined. ATP enhanced the activity of polyphe synthesis even at high concentrations of GTP, suggesting a specific role of ATP. At low concentrations of GTP, the extent of inhibition by AMP-P(NH)P was very low, probably owing to the prevention of the reduction of the GTP concentration. (iv) Vanadate inhibited the translocation reaction by high KCl-washed polysomes. These findings together indicate that ribosomal ATPase participates in peptide translation by inducing positive conformational changes of mammalian ribosomes, in addition to its role of chasing tRNA from the E site.

Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation. Publishing Authors By Initials

K Ogata,R Ohno,K Terao,K Iwasaki,Y Endo,

For similar inorganic chemicals: electrolytes: ions: anions: vanadates research abstracts see: inorganic chemicals: electrolytes: ions: anions: vanadates research

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Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 127

Page Numbers: 221-31

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 2000

Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation. Keywords Mesh Terms:

KEYWORDS: Vanadates

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation. Information

Substance Name: Adenosine Triphosphatases

Registry Number: EC 3.6.1.-

Grant and Affiliation Information for Some properties and the possible role of intrinsic ATPase of rat liver 80S ribosomes in peptide bond elongation.

AFFILIATION: Institute for Gene Expression, Dobashi Kyoritsu Hospital, Dobashi Matsuyama, Ehime 790-0032, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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