Skip to main content
PMC home page
Genetics logoLink to Genetics
. 1987 Jun;116(2):313–320. doi: 10.1093/genetics/116.2.313

Altered Turnover of Hypoxanthine Phosphoribosyltransferase in Erythroid Cells of Mice Expressing Hprt a and Hprt b Alleles

Gerald G Johnson 1,2, Verne M Chapman 1,2
PMCID: PMC1203141  PMID: 3609725

Abstract

We have previously shown that mice expressing Hprt a allele(s) have erythrocyte hypoxanthine phosphoribosyltransferase (HPRT) levels that are approximately 25-fold (Mus musculus castaneus) and 70-fold ( Mus spretus) higher than in mice that express the Hprt b allele (Mus musculus domesticus; C57BI/6J; C3H/HeHa), and that these differences in erythrocyte HPRT levels are due to differences in the turnover rates of the HPRT A and B proteins as reticulocytes mature to erythrocytes. We show here that: (1) the taxonomic subgroups of the genus Mus are essentially monomorphic for the occurrence of either the Hprt a or the Hprt b allele, with Hprt a being common in the aboriginal species (M. spretus, Mus hortulanus and Mus abbotti) and in several commensal species (Mus musculus musculus, M. m. castaneus, Mus musculus molossinus), while Hprt b is common in feral M. m. domesticus populations as well as in all inbred strains of mice tested; (2) in all these diverse Mus subgroups there is a strict association of Hprt a with high and Hprt b with low levels of erythrocyte HPRT; and, (3) the association between the occurrence of the Hprt a allele and elevated erythrocyte HPRT levels is retained following repeated backcrosses of wild-derived Hprt a allele(s) into the genetic background of inbred strains of mice with the Hprt b allele. Collectively, these observations indicate that the elevated and low levels of erythrocyte HPRT are specified by differences in the Hprt a and b structural genes. Since evidence indicates that Hprt a and b encode HPRT proteins which differ in primary structure, we infer that the structure of HPRT is an important factor in determining its sensitivity to turnover in mouse erythroid cells. Hprt a and b may provide a useful system of "normal" allelic gene products for identifying factors that participate in protein turnover during mouse reticulocyte maturation.

Full Text

The Full Text of this article is available as a PDF (738.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bonhomme F., Catalan J., Britton-Davidian J., Chapman V. M., Moriwaki K., Nevo E., Thaler L. Biochemical diversity and evolution in the genus Mus. Biochem Genet. 1984 Apr;22(3-4):275–303. doi: 10.1007/BF00484229. [DOI] [PubMed] [Google Scholar]
  2. Chapman V. M., Kratzer P. G., Quarantillo B. A. Electrophoretic variation for X chromosome-linked hypoxanthine phosphoribosyl transferase (HPRT) in wild-derived mice. Genetics. 1983 Apr;103(4):785–795. doi: 10.1093/genetics/103.4.785. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Chapman V. M., Nichols E. A., Ruddle F. H. Esterase-8 (Es-8): characterization, polymorphism, and linkage of an erythrocyte esterase locus on chromosome 7 of Mus musculus. Biochem Genet. 1974 May;11(5):347–358. doi: 10.1007/BF00486408. [DOI] [PubMed] [Google Scholar]
  4. Chapman V. M., Ruddle F. H. Glutamate oxaloacetate transaminase (got) genetics in the mouse: polymorphism of got-1. Genetics. 1972 Feb;70(2):299–305. doi: 10.1093/genetics/70.2.299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Chapman V. M., Shows T. B. Somatic cell genetic evidence for X-chromosome linkage of three enzymes in the mouse. Nature. 1976 Feb 26;259(5545):665–667. doi: 10.1038/259665a0. [DOI] [PubMed] [Google Scholar]
  6. Ciechanover A., Wolin S. L., Steitz J. A., Lodish H. F. Transfer RNA is an essential component of the ubiquitin- and ATP-dependent proteolytic system. Proc Natl Acad Sci U S A. 1985 Mar;82(5):1341–1345. doi: 10.1073/pnas.82.5.1341. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ferris S. D., Sage R. D., Prager E. M., Ritte U., Wilson A. C. Mitochondrial DNA evolution in mice. Genetics. 1983 Nov;105(3):681–721. doi: 10.1093/genetics/105.3.681. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Francke U., Lalley P. A., Moss W., Ivy J., Minna J. D. Gene mapping in Mus musculus by interspecific cell hybridization: assignment of the genes for tripeptidase-1 to chromosome 10, dipeptidase-2 to chromosome 18, acid phosphatase-1 to chromosome 12, and adenylate kinase-1 to chromosome 2. Cytogenet Cell Genet. 1977;19(2-3):57–84. doi: 10.1159/000130799. [DOI] [PubMed] [Google Scholar]
  9. Hershko A., Heller H., Elias S., Ciechanover A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J Biol Chem. 1983 Jul 10;258(13):8206–8214. [PubMed] [Google Scholar]
  10. Hunt W. G., Selander R. K. Biochemical genetics of hybridisation in European house mice. Heredity (Edinb) 1973 Aug;31(1):11–33. doi: 10.1038/hdy.1973.56. [DOI] [PubMed] [Google Scholar]
  11. Johnson G. G., Larsen T. A., Blakely P., Chapman V. M. Elevated levels of erythrocyte hypoxanthine phosphoribosyltransferase associated with allelic variation of murine Hprt. Biochemistry. 1985 Sep 10;24(19):5083–5089. doi: 10.1021/bi00340a019. [DOI] [PubMed] [Google Scholar]
  12. Konecki D. S., Brennand J., Fuscoe J. C., Caskey C. T., Chinault A. C. Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese hamster: construction and sequence analysis of cDNA recombinants. Nucleic Acids Res. 1982 Nov 11;10(21):6763–6775. doi: 10.1093/nar/10.21.6763. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lindahl K. F., Hausmann B., Chapman V. M. A new H-2-linked class I gene whose expression depends on a maternally inherited factor. Nature. 1983 Nov 24;306(5941):383–385. doi: 10.1038/306383a0. [DOI] [PubMed] [Google Scholar]
  14. Müller M., Dubiel W., Rathmann J., Rapoport S. Determination and characteristics of energy-dependent proteolysis in rabbit reticulocytes. Eur J Biochem. 1980 Aug;109(2):405–410. doi: 10.1111/j.1432-1033.1980.tb04808.x. [DOI] [PubMed] [Google Scholar]
  15. RABINOVITZ M., FISHER J. M. CHARACTERISTICS OF THE INHIBITION OF HEMOGLOBIN SYNTHESIS IN RABBIT RETICULOCYTES BY THREO-ALPHA-AMINO-BETA-CHLOROBUTYRIC ACID. Biochim Biophys Acta. 1964 Oct 16;91:313–322. doi: 10.1016/0926-6550(64)90255-5. [DOI] [PubMed] [Google Scholar]
  16. RIEDER R. F., ZINKHAM W. H., HOLTZMAN N. A. HEMOGLOBIN ZUERICH; CLINICAL, CHEMICAL AND KINETIC STUDIES. Am J Med. 1965 Jul;39:4–20. doi: 10.1016/0002-9343(65)90241-x. [DOI] [PubMed] [Google Scholar]
  17. Schimke R. T., Doyle D. Control of enzyme levels in animal tissues. Annu Rev Biochem. 1970;39:929–976. doi: 10.1146/annurev.bi.39.070170.004433. [DOI] [PubMed] [Google Scholar]

Articles from Genetics are provided here courtesy of Oxford University Press

RESOURCES