Chicken Brain Glutamine Synthetase and Comparison with Chicken Liver Mitochondrial Glutamine Synthetase*

Subcellular location of chicken brain glutamine synthetase and comparison with chicken liver mitochondrial glutamine synthetase.

Chicken brain glutamine synthetase has been found to be localized in the cytosolic fraction of this tissue in contrast to its mitochondrial location in chicken liver. Despite this difference in subcellular distribution, the enzyme from brain exhibits the same molecular weight during sodium dodecyl sulfate-polyacrylamide gel electrophoresis, has the same isoelectric point, and is immunochemicall...

Metabolic compartmentation of vertebrate glutamine synthetase: putative mitochondrial targeting signal in avian liver glutamine synthetase.

The evolution of uricoteley as a mechanism for hepatic ammonia detoxication in vertebrates required targeting of glutamine synthetase (GS) to liver mitochondria in the sauropsid line of descent leading to the squamate reptiles and archosaurs. Previous studies have shown that in birds and crocodilians, sole survivors of the archosaurian line, hepatic GS is translated without a transient, N-termi...

Biochemical and molecular analysis of glutamine synthetase gene in brassica napus L.

Weak mitochondrial targeting sequence determines tissue-specific subcellular localization of glutamine synthetase in liver and brain cells.

Evolution of the uricotelic system for ammonia detoxification required a mechanism for tissue-specific subcellular localization of glutamine synthetase (GS). In uricotelic vertebrates, GS is mitochondrial in liver cells and cytoplasmic in brain. Because these species contain a single copy of the GS gene, it is not clear how tissue-specific subcellular localization is achieved. Here we show that...

Inactivation of glutamine synthetases by an NAD:arginine ADP-ribosyltransferase.

Glutamine synthetase from ovine brain has a critical arginine residue at the catalytic site (Powers, S. G., and Riordan, J.F. (1975) Proc. Natl. Acad. Sci. U.S. A. 72, 2616-2620). This enzyme is now shown to be a substrate for a purified NAD:arginine ADP-ribosyltransferase from turkey erythrocyte cytosol that catalyzes the transfer of ADP-ribose from NAD to arginine and purified proteins. The t...