Unilateral aminoacylation specificity between bovine mitochondria and eubacteria.

Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. Research Abstract Details 

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Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. Abstract Text:

Y Kumazawa,H Himeno,K Miura,K Watanabe,

The present study shows unilateral aminoacylation specificity between bovine mitochondria and eubacteria (Escherichia coli and Thermus thermophilus) in five amino acid-specific aminoacylation systems. Mitochondrial synthetases were capable of charging eubacterial tRNA as well as mitochondrial tRNA, whereas eubacterial synthetases did not efficiently charge mitochondrial tRNA. Mitochondrial phenylalanyl-, threonyl-, arginyl-, and lysyl-tRNA synthetases were shown to charge and discriminate cognate E. coli tRNA species from noncognate ones strictly, as did the corresponding E. coli synthetases. By contrast, mitochondrial seryl-tRNA synthetase not only charged cognate E. coli serine tRNA species but also extensively misacylated noncognate E. coli tRNA species. These results suggest a certain conservation of tRNA recognition mechanisms between the mitochondrial and E. coli aminoacyl-tRNA synthetases in that anticodon sequences are most likely to be recognized by the former four synthetases, but not sufficiently by the seryl-tRNA synthetase. The unilaterality in aminoacylation may imply that tRNA recognition mechanisms of the mitochondrial synthetases have evolved to be, to some extent, simpler than their eubacterial counterparts in response to simplifications in the species-number and the structural elements of animal mitochondrial tRNAs.

Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. Publishing Authors By Initials

Y Kumazawa,H Himeno,K Miura,K Watanabe,

For similar bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus research abstracts see: bacteria: gram-negative bacteria: gram-negative aerobic bacteria: gram-negative aerobic rods and cocci: thermus research

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Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 109

Page Numbers: 421-7

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Mar

YEAR: 1991

Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. Keywords Mesh Terms:

KEYWORDS: Thermus

MESH TERMS: genetics

Chemical & Substance for Abstract: Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. Information

Substance Name: Amino Acyl-tRNA Synthetases

Registry Number: EC 6.1.1.-

Grant and Affiliation Information for Unilateral aminoacylation specificity between bovine mitochondria and eubacteria.

AFFILIATION: Department of Biological Sciences, Tokyo Institute of Technology, Kanagawa.

Country: JAPAN

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MEDLINETA: J Biochem

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