Abstract
It is now generally accepted that the composition of biological membranes is under genetic control. For each membrane protein, each enzyme involved in the biosynthesis of membrane lipids, and each enzyme that modifies either proteins or lipids (e.g., by adding carbohydrate residues to make glycoproteins or glycolipids), there must be a structural gene whose nucleotide sequence specifies the appropriate amino acid sequence. In addition, there are assumed to be regulatory genes which govern the rates at which the various proteins are made. The purpose of this chapter is to survey the ways in which genetic studies can contribute to our understanding of membrane structure and function. Successive sections of the chapter will discuss the criteria for establishing that differences in membrane properties are genetically determined, the kinds of information that can come from biochemical and physiological studies on membrane mutants, and the information that can be gained by genetic analysis. First, however, it will be important to define the various mutational events that can occur, and the effects of each on the structure or rate of synthesis of the corresponding protein.
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References
Abrams, M., and J. D. Battle, Jr. 1952. A genetic study in hereditary spherocytosis. Am. J. Hum. Genet. 4: 350–355.
Adler, J., and W. Epstein. 1974. Phosphotransferasesystem enzymes as chemoreceptors for certain sugars in Escherichia coli chemotaxis. Proc. Natl. Acad. Sci. U.S.A. 71: 2895–2899.
Adler, J., G. L. Hazelbauer, and M. M. Dahl. 1973. Chemotaxis toward sugars in Escherichia coli. J. Bacteriol. 115: 824–847.
Aksamit, R., and D. E. Koshland, Jr. 1972. A ribose binding protein of Salmonella typhimurium. Biochem. Biophys. Res. Commun. 48: 1348–1353.
Ames, G. F. 1964. Uptake of amino acids by Salmonella typhimurium. Arch. Biochem. Biophys. 104: 1–18.
Ames, G. F., and J. Lever. 1970. Components of histidine transport: Histidine-binding proteins and hisP protein. Proc. Natl. Acad. Sci. U.S.A. 66: 1096–1103.
Ames, G. F., and J. Lever. 1972. The histidine-binding protein J is a component of histidine transport: Identification of its structural gene hisJ. J. Biol. Chem. 247: 4309–4316.
Baker, R. M., D. M. Brunette, R. Mankovitz, L. H. Thompson, G. F. Whitmore, L. Simonovitch, and J. E. Till. 1974. Ouabain-resistant mutants of mouse and hamster cells in culture. Cell 1: 9–21.
Beckwith, J. R., and D. Zipser, eds. 1970. The Lactose Operon. Cold Spring Harbor Laboratory, New York.
Boos, W. 1972. Structurally defective galactose-binding protein isolated from a mutant negative in the ßmethylgalactoside transport System of Escherichia coli J. Biol. Chem. 247: 5414–5424.
Boos, W. 1974. Pro and contra carrier proteins; sugar transport via the periplasmic galactose-binding protein. In: Current Topics in Membranes and Transport, Vol. 5. F. Bronner and A. Kleinzeller, eds. Academic Press. New York. pp. 51–136.
Chasin, L. A. 1973. The effect of ploidy on chemical mutagenesis in cultured Chinese hamster cells. J. Cell. Physiol. 82: 299–308.
Dunham, P. B., and J. F. Hoffman. 1971. Active cation transport and ouabain binding in high potassium and low potassium red blood cells of sheep. J. Gen. Physiol. 58: 94–116.
Elsas, L. J., R. E. Hillman, J. H. Patterson, and L. E. Rosenberg. 1970. Renal and intestinal hexose transport in familial glucose-galactose malabsorption. J. Clin. Invest. 49: 576–585.
Ephrussi. B. 1972. Hybridization of Somatic Cells. Princeton Univ. Press, Princeton, New Jersey.
Fox, C. F., J. R. Carter, and E. P. Kennedy. 1967. Genetic control of the membrane protein component of the lactose transport system of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 57: 698–705.
Fox, C. F., and E. P. Kennedy. 1965. Specific labelling and partial purification of the M protein, a component of the ß-galactoside transport system of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 54: 891–899.
Harris, H. 1970. Cell Fusion. Oxford Univ. Press ( Clarendon ), London.
Hazelbauer, G. L., and J. Adler. 1971. Role of the galactose binding protein in chemotaxis of Escherichia coli toward galactose. Nature (New Biol.) 230: 101–104.
Hoffman, P. G., and D. C. Tosteson. 1971. Active sodium and potassium transport in high potassium and low potassium sheep red cells. J. Gen. Physiol. 58: 438–466.
Jacob, F., D. Perrin, C. Sanchez, and J. Monod. 1960. L’opéron: Groupe de gènes à expression coordonée par un opérateur. C. R. Acad. Sci. 250: 1727–1729.
Jones, T. H. D., and E. P. Kennedy. 1969. Characterization of the membrane protein component of the lactose transport system of Escherichia coli. J. Biol. Chem. 244: 5981–5987.
Kennedy, E. P. 1970. The lactose permease system of Escherichia coli. In: The Lactose Operon. J. R. Beckwith and D. Zipser, eds. Cold Spring Harbor Laboratory, New York. pp. 49–82.
Kennedy, E. P., M. K. Rumley, and J. B. Armstrong. 1974. Direct measurement of the binding of labeled sugars to the lactose permease M protein. J. Biol. Chem. 249: 33–37.
Kung, C., S.-Y. Chang, Y. Satow. J. Van Houten, and H. Hansma. 1975. Genetic dissection of behavior in Paramecium. Science 188: 898–904.
Kustu, S. G., and G. F. Ames. 1974. The histidine-binding protein J, a histidine transport component, has two different functional sites. J. Biol. Chem. 249: 69766983.
Lever, J. E. 1972. Purification and properties of a component of histidine transport in Salmonella typhimurium: The histidine-binding protein J. J. Biol. Chem. 247: 4317–4326.
Mankovitz, R., M. Buchwald, and R. M. Baker. 1974. Isolation of ouabain-resistant human diploid fibroblasts. Cell 3: 221–226.
Mezger-Freed, L. 1971. Puromycin-resistance in haploid and heteroploid frog cells: Gene or membrane determined? J. Cell Biol. 51: 742–751.
Ordal, G. W., and J. Adler. 1974. Isolation and complementation of mutants in galactose taxis and transport. J. Bacteriol. 117: 509–516.
Orda!, G. W., and J. Adler. 1974. Properties of mutants in galactose taxis and transport. J. Bacteriol. 117: 517526.
Rosenberg, L. E., and C. R. Scriver. 1974. Disorders of amino acid metabolism. In: Duncan’s Diseases of Metabolism, 7th ed. P. K. Bondy and L. E. Rosenberg, eds. Saunders, Philadelphia, Pennsylvania. pp. 465–654.
Slayman, C. W. 1973. The genetic control of membrane transport. In: Current Topics in Membranes and Transport, Vol. 4. F. Bronner and A. Kleinzeller, eds. Academic Press, New York. pp. 1–174.
Stanley, P., V. Caillibot, and L. Simonovitch. 1975. Stable alterations at the cell membrane of Chinese hamster ovary cells resistant to the cytotoxicity of phytohemagglutinin. Somatic Cell Genet. 1: 3–26.
Stanley, P., S. Narasimhan, L. Siminovitch, H. Schacter. 1975. Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine-glycoprotein N-acetylglucosaminyl transferase activity. Proc. Natl. Acad. Sci. U.S.A. 72: 3323–3327.
Till, J. E., R. M. Baker, D. M. Brunette, V. Ling, L. H. Thompson, and J. A. Wright. 1973. Genetic regulation of membrane function in mammalian cells in culture. Fed. Proc. 32: 29–33.
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Adelberg, E.A., Slayman, C.W. (1980). Genes and Membranes. In: Andreoli, T.E., Hoffman, J.F., Fanestil, D.D. (eds) Membrane Physiology. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1718-1_19
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DOI: https://doi.org/10.1007/978-1-4757-1718-1_19
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