High molecular weight complex formation of rat liver lysyl-tRNA synthetase reduces enzyme lability to thermal inactivation

Chi V. Dang

doi:10.1016/0006-291X(82)92055-1

High molecular weight complex formation of rat liver lysyl-tRNA synthetase reduces enzyme lability to thermal inactivation

Chi V. Dang

School of Medicine

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

Eukaryotic aminoacyl-tRNA synthetases tend to occur in high molecular weight multienzyme complexes in contrast to the prokaryotic counterparts. The functional significance of complex formation is not understood but stabilization of enzyme activities in the complex(es) has been suggested as one of many possible functions. We provide evidence that the 24S complex lysyl-tRNA synthetase activity is more resistant to thermal inactivation than the 6S free lysyl-tRNA synthetase activity at 30°, 37°, and 43°C.

Original language	English (US)
Pages (from-to)	44-47
Number of pages	4
Journal	Biochemical and Biophysical Research Communications
Volume	106
Issue number	1
DOIs	https://doi.org/10.1016/0006-291X(82)92055-1
State	Published - May 14 1982

ASJC Scopus subject areas

Molecular Biology
Biophysics
Biochemistry
Cell Biology

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10.1016/0006-291X(82)92055-1

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abstract = "Eukaryotic aminoacyl-tRNA synthetases tend to occur in high molecular weight multienzyme complexes in contrast to the prokaryotic counterparts. The functional significance of complex formation is not understood but stabilization of enzyme activities in the complex(es) has been suggested as one of many possible functions. We provide evidence that the 24S complex lysyl-tRNA synthetase activity is more resistant to thermal inactivation than the 6S free lysyl-tRNA synthetase activity at 30°, 37°, and 43°C.",

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AB - Eukaryotic aminoacyl-tRNA synthetases tend to occur in high molecular weight multienzyme complexes in contrast to the prokaryotic counterparts. The functional significance of complex formation is not understood but stabilization of enzyme activities in the complex(es) has been suggested as one of many possible functions. We provide evidence that the 24S complex lysyl-tRNA synthetase activity is more resistant to thermal inactivation than the 6S free lysyl-tRNA synthetase activity at 30°, 37°, and 43°C.

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High molecular weight complex formation of rat liver lysyl-tRNA synthetase reduces enzyme lability to thermal inactivation

Abstract

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