||Conservation of Structure in the Human Gene Encoding Argininosuccinate Synthetase and the argG Genes of the Archaebacteria 'Methanosarcina barkeri' MS and 'Methanococcus vannielii'.
Morris, C. J. ;
Reeve, J. N. ;
||Ohio State Univ., Columbus. Dept. of Microbiology.;Environmental Protection Agency, Cincinnati, OH. Risk Reduction Engineering Lab.;Office of Naval Research, Arlington, VA.;Department of Energy, Washington, DC.
||EPA-R-812774 ;N00014-86-K-0211; EPA/600/J-88/370;
Deoxyribonucleic acids ;
Escherichia coli ;
Methanosarcina barkeri MS ;
Methanococcus vannielii ;
Nucleic acid sequence homology ;
Argininosuccinate synthetase ;
Base sequence ;
Amino acid sequence ;
||Some EPA libraries have a fiche copy filed under the call number shown.
The DNA sequences of the argG genes of Methanosarcina barkeri MS and Methanococcus vannielii were determined. The polypeptide products of these methanogen genes have amino acid sequences which are 50% identical to each other and 38% identical to the amino acid sequence encoded by the exons of the human argininosuccinate synthetase gene. Introns in the human chromosomal gene separate regions which encode amino acids conserved in both the archaebacterial and human gene products. An open reading frame immediately upstream of argG in Methanosarcina barkeri MS codes for an amino acid sequence which is 45 and 31% identical to the sequences of the large subunits of carbamyl phosphate synthetase in Escherichia coli and Saccharomyces cerevisiae, respectively. If this gene encodes carbamyl phosphate synthetase in Methanosarcina barkeri, this is the first example in an archaebacterium of physical linkage of genes that encode enzymes which catalyze reactions in the same amino acid biosynthetic pathway. (Copyright (c) 1988, American Society of Microbiology.)