An immunological approach was used for the study of ornithine carbamoyltransferase (OTCase) evolution in bacteria. Antisera were prepared against the anabolic and catabolic OTCases of Pseudomonas aeruginosa and Aeromonas formicans as well as against OTCase and putrescine carbamoyltransferases from Streptococcus faecalis; these antisera were then tested against the unpurified OTCases, either anabolic or catabolic, of 34 bacterial strains. Extensive cross-reactions were observed between the antisera to catabolic OTCases from P. aeruginosa, A. formicans and S. faecalis and the catabolic enzymes from other species or genera. These antisera cross-reacted also with the anabolic OTCases of strains of the Enterobacteriaceae but not with the anabolic OTCases of the same species or of other species or genera. The cross-reaction measured between the antisera against P. aeruginosa anabolic OTCase and the anabolic OTCases of other Pseudomonas were largely in agreement with the phylogenic subdivision of Pseudomonas proposed by N. J. Palleroni. The correlation was also significantly higher with the anabolic enzyme of an archaeobacterium, Methanobacterium thermoaceticum, than with the catabolic or anabolic OTCases from other genera in the eubacterial line. The antiserum raised against A. formicans anabolic OTCase was quite specific for its antigen and appeared to be raised against the heaviest of the various oligomeric structures of the enzyme.
BaurH.,
StalonV.,
FalmagneP.,
LüthiE.,
HaasD.1987; Primary and quaternary structure of the catabolic ornithine carbamoyltransferase from Pseudomonas aeruginosa. Extensive sequence homology with the anabolic ornithine carbamoyltransferases of Escherichia coli
. European Journal of Biochemistry 166:111–117
BenciniD.A.,
HoughtonJ.E.,
HooverT.A.,
FoltermannK.F.,
WildJ.R.,
O’donovanG.A.1983; The DNA sequence of argI from E. coli K-12. Nucleic Acids Research 11:8509–8518
BernesteinF.C.,
KoetzleT.F.,
WilliamsG.J.B.,
MeyerE.F.JRBriceM.D.,
RodgersJ.R.,
KennardO.,
ShimanouchiT.,
TasumiM.1977; The protein data bank: a computer-based archival file for macromolecular structures. Journal of Biology 112:535–542
BromanK.,
LauwersN.,
StalonV.1978; Oxygen and nitrate in the utilization by Bacillus licheniformis of the arginase and arginine deiminase routes of arginine catabolism, and other factors affecting their synthesis. Journal of Bacteriology 135:920–927
ByngG.S.,
JohnsonJ.L.,
WhitakerR.J.,
GhernaR.,
JensenR.A.1983; The evolutionary pattern of aromatic amino acid biosynthesis and the emerging phylogeny of pseudomonad bacteria. Journal of Molecular Evolution 19:272–282
FalmagneP.,
PortetelleD.,
StalonV.1985; Immunological and structural relatedness of catabolic ornithine carbamoyltransferases and the anabolic enzymes of enterobacteria. Journal of Bacteriology 161:714–719
GoadW.B.,
KanehisaM.L.1982; Pattern recognition in nucleic acid sequences. A general method for finding local homologies and symmetries. Nucleic Acids Research 10:247–263
HalleuxP.,
LegrainC.,
StalonV.,
PierardA.,
WiameJ.M.1972; Regulation of the catabolic ornithine carbamoyltransferase of Pseudomonas fluorescens. A study of the quaternary structure. European Journal of Biochemistry 31:386–393
HooverT.A.,
RoofW.D.,
FoltermannK.F.,
O'donovanG.A.,
BenciniD.A.,
WildJ.R.1983; Nucleotide sequence of the structural gene ipyrB) that encodes the catalytic polypeptide of aspartate carbamoyltransferase of Escherichia coli
. Proceedings of the National Academy of Sciences of the United States of America 80:2462–2466
HoppT.P.,
WoodsR.1981; Prediction of protein antigenic determinants from amino acid sequences. Proceedings of the National Academy of Sciences of the United States of America 78:3824–3828
HuygenR.,
CrabeelM.,
GlansdorffN.1987; Nucleotide sequence of the ARG3 gene of the yeast Saccharomyces cerevisiae encoding ornithine carbamoyltransferase. European Journal of Biochemistry 166:371–377
ItohY.,
SoldatiL.,
StalonV.,
FalmagneP.,
TerawakiY.,
LeisingerT.,
HaasD.1988; Anabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa: nucleotide sequence and transcriptional control of the argF structural gene. Journal of Bacteriology 170:2725–2734
KimK.H.,
PanZ.,
HonzatkoR.B.,
KeH.M.,
LipscombW.N.1987; Structural asymmetry in the CTP-liganded form of aspartate carbamoyltransferase from Escherichia coli
. Journal of Molecular Biology 196:853–875
LegrainC.,
StalonV.1976; Ornithine carbamoyltransferase from Escherichia coli W. Purification, structure, and steady-state kinetic analysis. European Journal of Biochemistry 63:289–301
LegrainC.,
HalleuxP.,
StalonV.,
GlansdorffN.1972; The dual genetic control of ornithine carbamoyltransferase in Escherichia coli : a case of bacterial hybrid enzymes. European Journal of Biochemistry 27:93–102
LegrainC.,
StalonV.,
NoullezJ.P.,
MercenierA.,
SimonJ.P.,
BromanK.,
WiameJ.M.1977; Structure and function of ornithine carbamoyltransferases. European Journal of Biochemistry 80:401–409
LernerC.G.,
SwitzerR.L.1986; Cloning and structure of the Bacillus subtilis aspartate transcarba-moylase gene. Journal of Biological Chemistry 261:11156–11165
MarshallM.,
CohenP.P.1972; Ornithine transcarbamylase from Streptococcus faecalis and bovine liver: isolation and subunit structure. Journal of Biological Chemistry 247:1641–1653
MonacoH.L.,
CrawfordJ.L.,
LipscombW.N.1978; Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and its complex with cytidine triphosphate. Proceedings of the National Academy of Sciences of the United States of America 75:5276–5280
PalleroniN.J.,
KunisawaR.,
ContopoulouR.,
DoudoroffM.1974; Nucleic acid homologies in the genus Pseudomonas
. International Journal of Systematic Bacteriology 23:333–339
PearsonW.R.,
LipmanD.J.1988; Improved tools for biological sequences comparison. Proceedings of the National Academy of Sciences of the United States of America 85:2444–2448
StalonV.,
RamosF.,
PierardA.,
WiameJ.M.1972; Regulation of the catabolic ornithine carbamoyltransferase of Pseudomonas fluorescens: a comparison with the anabolic transferase and with a mutationally modified catabolic transferase. European Journal of Biochemistry 29:25–35
Van vlietF.,
CuninR.,
JacobsA.,
PietteJ.,
GigotD.,
LauwereysM.,
PierardA.,
GlansdorffN.1984; Evolutionary divergence of genes for ornithine and aspartate carbamoyltransferases-complete sequence and mode of regulation of the Escherichia coli argF gene; comparison of argF with argI and pyrB
. Nucleic Acids Research 12:6277–6289
Van vlietF.,
BoyenA.,
GlansdorffN.1988; On interspecies gene transfer: the case of the argF gene of Escherichia coli
. Annales de I'Institut Pasteur I Microbiologie 139:493–496
WargniesB.,
LauwersN.,
StalonV.1979; Structure and properties of the putrescine carbamoyltransferase of Streptococcus faecalis
. European Journal of Biochemistry 101:145–152
WesthofE.,
AltshuhD.,
MorasD.,
BloomerA.C.,
MondragonA.,
KlugA.,
Vanregen-MORTELM.H.V.1984; Correlation between segmental mobility and the location of antigenic determinants in proteins. Nature; London: 311123–134