Joshi, Anil K and Cherayil, Joseph D (1987) Stabilization of some of the protein synthesis components in the thermophilic fungus, Humicola lanuginosa. In: Journal of Biosciences, 11 (1-4). pp. 193-202.Full text not available from this repository. (Request a copy)
The thermal stabilities of the tRNA from the thermophilic fungus Humicoal lanuginosa were compared with that from the mesophilic yeast Candida utilis by measuring the increase in the optical d. with temp. The tRNAs from both species were stable in the presence of millimolar quantities of $MgCl_2$ to 50%, the optimum growth temp. of the fungus. Aminoacyl-tRNA synthetases were maximally active at 40 under the in vitro assay conditions. They were fractionated, and one species of valine tRNA synthetase was purified to homogeneity. The purified enzyme was protected against inactivation to varying degrees when preincubated with the substrates valine, tRNA, and ATP as well as spermine. Protein turnover studies showed that the rate of turnover was higher at higher temps. Thus, the protein-synthesizing machinery of this fungus has no intrinsic stability by intracellular factors. A higher rate of protein turnover also plays a role for growth at higher temp.
|Item Type:||Journal Article|
|Additional Information:||Copyright belongs to The Indian Academy of Sciences|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||18 Mar 2008|
|Last Modified:||27 Aug 2008 13:14|
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