Summary
The localization of the human genes for cytosolic and mitochondrial aspartate aminotransferase (AspAT) has been determined by chromosomal in situ hybridization with specific human cDNA probes previously characterized in our laboratory. The cytosolic AspAT gene is localized on chromosome 10 at the interface of bands q241–q251. Mitochondrial AspAT is characterized by a multigene family located on chromosomes 12 (p131–p132), 16 (q21), and 1 (p32–p33 and q25–q31). Genomic DNA from ten blood donors was digested by ten restriction enzymes, and Southern blots were hybridized with the two specific probes. Restriction fragment length polymorphism was revealed in only one case for cytosolic AspAT, with PvuII, while no polymorphism for mitochondrial AspAT was found.
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References
Aitken DA, Ferguson-Smith MA (1978) Gene dosage evidence for the regional assignment of the GOTs structural gene locus to 10q24→10q25 Cytogenet Cell Genet 22: 468–471
Blin N, Stafford DW (1976) A general method for isolation of high molecular weight DNA from eukaryotes. Nucleic Acids Res 9: 2303–2308
Braunstein AE (1985) Transamination and transaminases. In: Christen P, Metzler DE (eds) Transaminases. Wiley, New York, pp 2–19
Chern CJ, Mellman WJ, Croce CM (1976) Localization of the structural locus for cytoplasmic glutamic-oxaloacetic transaminase to region q24→qter of human chromosome 10. Cytogenet Cell Genet 16: 108–110
Cooper AJL, Meister A (1985) Metabolic significance of transamination. In: Christen P, Metzler DE (eds) Transaminases. Wiley, New York, pp 534–563
Craig IW, Tolley E, Bobrow M, Heyningen V van (1978) Assignment of a gene necessary for the expression of mitochondrial glutamicoxaloacetic transaminase in human-mouse hybrid cells. Cytogenet Cell Genet 22: 190–194
Davidson RG, Cortner JA, Rattazzi MC, Ruddle FH, Lubs HA (1970) Genetic polymorphism of human mitochondrial glutamic oxaloacetic transaminase. Science 169: 391–392
Duncan IW, Scott EM, Wright RC (1974) Gene frequencies of erythrocytic enzymes of Alaskan Eskimos and Athabaskan Indians. Am J Hum Genet 26: 244–246
Hackel E, Hopkinson DA, Harris H (1972) Population studies on mitochondrial glutamate-oxaloacetate transaminase. Ann Hum Genet 35: 491–496
Jeremiah SJ, Povey S, Burley NW, Kietly C, Lee M, Spowart G, Corney G, Cook PJL (1982) Mapping studies on human mitochondrial glutamate oxaloacetate transaminase. Ann Hum Genet 35: 145–152
Maniatis T, Fritsch EF, Sambrook J (eds) (1982) Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
Mattei MG, Philip N, Passage E, Moisan JP, Mandel JL, Mattei JF (1985) DNA probe localization at 18p113 band by in situ hybridization and identification of a small supernumerary chromosome. Hum Genet 69: 268–271
Mitchell G, Valle D, Willard H, Steel G, Suchaneck M, Brody L (1986) Human ornithine-delta-aminotransferase (OAT): cross-hybridizing fragments mapped to chromosome 10 and Xp11.1-21.1 (abstract). Am J Hum Genet 36: A163
Mouse News Letter (1987) Mouse chromosome atlas, map of mouse, man homologies. Mouse News Lett 78: 12–26
Nalpas B, Vassault A, Charpin S, Lacour B, Berthelot P (1986) Serum mitochondrial aspartate aminotransferase as a marker of chronic alcoholism: diagnostic value and interpretation in a liver unit. Hepatology 6: 608–614
Obaru K, Tsuzuki T, Setoyama C, Shimada K (1988) Structural organization of the mouse aspartate aminotransferase isoenzyme genes. Introns antedate the divergence of cytosolic and mitochondrial isoenzyme genes. J Mol Biol 200: 13–22
Okuno F, Ishii H, Kashiwazaki K, Takagi S, Shigeta Y, Arai M, Takagi T, Ebihara Y, Tsuchiya M (1988) Increase in mitochondrial GOT (m-GOT) activity after chronic alcohol consumption clinical and experimental observations. Alcohol 5: 49–53
Pavé-Preux M, Ferry N, Bouguet J, Hanoune J, Barouki R (1988) Nucleotide sequence and glucocorticoid regulation of the mRNAs for the isoenzymes of rat aspartate aminotransferase. J Biol Chem 263: 17459–17466
Pol S, Bousquet-Lemercier B, Pavé-Preux M, Pawlak A, Berthelot P, Hanoune J, Barouki R (1988) Nucleotide sequence and tissue distribution of mitochondrial aspartate aminotransferase mRNA. Biochem Biophys Res Commun 157: 1309–1315
Ramesh V, Eddy R, Shows TB, Shih VE, Gusella JF (1986) Chromosomal assignment of human ornithine aminotransferase (abstract). Am J Hum Genet 39: A166
Ritter H, Kömpf J (1979) Human mitochondrial glutamic-oxaloacetic-transaminase, GOTM: formal genetics. Hum Genet 51: 327–329
Roderick TH, Davisson MT (1984) In: O'Brien SJ (ed) Genetic maps, vol 3. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, pp 343–356
Sonderegger P, Jaussi R, Christen P, Gehring H (1982) Biosynthesis of aspartate aminotransferases. Both the higher molecular weight precursor of mitochondrial aspartate aminotransferase and the cytosolic isoenzyme are synthesized on free polysomes. J Biol Chem 257: 3339–3345
Southern EJ (1975) Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol 98: 503–517
Spritz RA, Emanuel BS, Chern CJ, Mellman WJ (1979) Gene dosage effect: intraband mapping of human soluble glutamic oxaloacetic transaminase. Cytogenet Cell Genet 23: 149–156
Tolley E, Van Heyningen V, Brown R, Bobrow M, Craig IW (1980) Assignment to chromosome 16 of a gene necessary for the expression of human mitochondrial glutamate oxaloacetate transaminase (aspartate aminotransferase) (E.C.2.6.1.1.). Biochem Genet 18: 947–954
Tsuzuki T, Obaru K, Setoyama C, Shimada K (1987) Structural organization of the mouse mitochondrial aspartate aminotransferase gene. J Mol Biol 198: 21–31
Wahl CR, Stern M, Stark G (1979) Efficient transfer of large DNA fragments from agarose gels to diazobenzyloxymethyl-paper and rapid hybridization by using dextran sulfate. Proc Natl Acad Sci USA 76: 3683–3687
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Pol, S., Bousquet-Lemercier, B., Pavé-Preux, M. et al. Chromosomal localization of human aspartate aminotransferase genes by in situ hybridization. Hum Genet 83, 159–164 (1989). https://doi.org/10.1007/BF00286710
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DOI: https://doi.org/10.1007/BF00286710