Abstract
The amylase complex on mouse chromosome 3 encodes both salivary and pancreatic amylase. It appears that one active gene is present for salivary amylase, whereas pancreatic amylase in some strains is coded by at least 4, and perhaps by more than 10, genes. Strain YBR is different from other strains in that it produces twice as much salivary amylase. Pancreatic amylase in YBR is present as two different protein forms, Aβ and Bβ, the sum of which amounts to only one-third of that in, for instance, strain A/J. YBR chromosomal DNA was cloned in phage λ, followed by restriction and heteroduplex analysis of recombinant phages carrying amylase genes. Among 32 phage isolates, 5 carried parts of the salivary amylase sequence. The remaining phage isolates contained pancreatic amylase-like sequences and represented three nonoverlapping genomic regions, i.e., one of 34 kb containing a complete gene, PAN-IIβ; another of 41 kb with a complete but different gene, PAN-Iβ, plus a truncated gene, PAN-ψ1; and finally, one of 23 kb with another truncated gene, PAN-ψ2. Parts of the amino acid sequence of Aβ and Bβ have previously been determined, and we report here the sequencing of a 4-kb DNA fragment from Pan-IIβ which establishes that this gene codes for Bβ.
Similar content being viewed by others
References
Belayew, A., and Tilghman, S. M. (1982). Genetic analysis of α-fetoprotein synthesis in mice. Mol. Cell. Biol. 21427.
Biggin, M. D., Gibson, T. J., and Honk, G. F. (1983). Buffer gradient gels and 35S label as an aid to rapid DNA sequence determination. Proc. Natl. Acad. Sci. USA 803963.
Bloor, J. H., Meisler, M. H., and Nielsen, J. T. (1981). Genetic determination of amylase synthesis in the mouse. J. Biol. Chem. 256373.
Christiansen, G., and Christiansen, C. (1983). Heterology of mitochondrial DNA from mammals detected by microscopic heteroduplex analysis. Nucl. Acids Res. 1137.
Crerar, M., Swain, W. F., Pictet, R. L., Nikovits, W., and Rutter, W. J. (1983). Isolation and characterization of a rat amylase gene family. J. Biol. Chem. 2581311.
Deininger, P. (1983). Random subcloning of sonicated DNA: Application to shotgun DNA sequence analysis. Anal. Biochem. 129216.
Eicher, E. M., and Lane, P. W. (1980). Assignment of LG XVI to chromosome 3 in the mouse. J. Hered. 71315.
Girvitz, S. C., Bacchetti, S., Rainbow, A. J., and Graham, F. L. (1980). A rapid and efficient procedure for the purification of DNA from agarose gels. Anal. Biochem. 106492.
Grosveld, F. G., Dahl, H.-H. M., Boer, E., and Flavell, R. A. (1981). Isolation of β-globin-related genes from a human cosmid library. Gene 13227.
Hagenbüchle, O., Bovey, R., and Young, R. A. (1980). Tissue-specific expression of mouse α-amylase genes: Nucleotide sequence of isoenzyme mRNAs from pancreas and salivary gland. Cell 21179.
Hagenbüchle, O., Wellauer, P. K., Cribbs, D. L., and Schibler, U. (1984). Termination of transcription in the mouse α-amylase gene Amy-2 a occurs at multiple sites downstream of the polyadenylation site. Cell 38737.
Hjorth, J. P. (1979). Genetic variation in mouse salivary amylase rate of synthesis. Biochem. Genet. 17665.
Hjorth, J. P. (1982). Altered salivary amylase gene in the mouse strain BXD-16. Heredity 48127.
Hjorth, J. P., Lusis, A. J., and Nielsen, J. T. (1980). Multiple structural genes for mouse amylase. Biochem. Genet. 18281.
Jeffreys, A. J., Barrie, P. A., Harris, S., Fawcett, D. H., Nugent, Z. J., and Boyd, A. C. (1982). Isolation and sequence analysis of a hybrid δ-globin pseudo gene from the Brown lemur. J. Mol. Biol. 156487.
Larson, R., and Messing, J. (1982). Apple II software for M13 shotgun DNA sequencing. Nucl. Acids Res. 1039.
Loenen, W. A. M., and Brammar, W. J. (1980). A bacteriophage lambda vector for cloning large DNA fragments made with several restriction enzymes. Gene 20249.
Messing, J. (1983). New M13 vectors for cloning. Methods Enzymol. 10120.
Nielsen, J. T. (1982). Variation in amylase haplotypes among congenic lines of the house mouse. Genetics 102571.
Rigby, P. W. J., Dieckman, M., Rhodes, C., and Berg, P. (1977). Labelling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J. Mol. Biol. 113237.
Sanger, F., Nicklen, S., and Coulson, A. R. (1977). DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 745463.
Schibler, U., Tosi, M., Pittet, A.-C., Fabiani, L., and Wellauer, P. K. (1980). Tissue-specific expression of mouse alpha-amylase genes. J. Mol. Biol. 14293.
Schibler, U., Pittet, A.-C., Young, R. A., Hagenbüchle, O., Tosi, M., Gellman, S., and Wellauer, P. K. (1982). The mouse α-amylase multigene family. Sequence organization of members expressed in the pancreas, salivary gland and liver. J. Mol. Biol. 155247.
Southern, E. M. (1980). Detection of specific sequences among DNA fragments separated by gel electrophoresis. Methods Enzymol. 68152.
Strahler, J. R., and Meisler, M. H. (1982). Two distinct pancreatic amylase genes are active in YBR mice. Genetics 10191.
Thomsen, K. K., Hjorth, J. P., and Nielsen, J. T. (1984). Genetic variation in restriction patterns among mouse amylase gene complexes. Biochem. Genet. 22257.
Author information
Authors and Affiliations
Additional information
This work was supported by the Danish Natural Science Research Council.
Rights and permissions
About this article
Cite this article
Mikkelsen, B.M., Clark, M.E., Christiansen, G. et al. The structure of two distinct pancreatic amylase genes in mouse strain YBR. Biochem Genet 23, 511–524 (1985). https://doi.org/10.1007/BF00504287
Received:
Revised:
Issue Date:
DOI: https://doi.org/10.1007/BF00504287