Abstract
Preparative isoelectric focusing was used to separate free bacterial NAD+ nucleosidase from its complex with a bound host component. Both fractions were characterized by optimum temperature and activation energy of denaturation. The bacterial product is enzymically inactive. The enzymically active structure is formed upon binding to the host component. Only the host organism can provide the suitable, activating structure. The host component in the present system is added to the cultivation medium with a beef heart extract but it can be replaced by serum albumin. The possible role of albumin as a carrier structure for flexible and enzymically inactive peptides is discussed. Different peptides bound to albumin can provide different enzyme activities. The term binary enzyme is coined, referring to a situation where the two enzyme components are coded at genetically distant loci. The pathogen makes use of the carrier structure of albumin type and produces another polypeptide invested with an enzyme activity convenient for the pathogen.
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References
Anai M., Haraguchi H., Takagi Y.: An endonuclease associated with bovine plasma albumin fraction. I. Purification and some properties of the enzyme.J. Biol. Chem. 247, 193–198 (1972).
Carlson A.S., Kellner A., Bernheimer A.W., Freeman E.B.: A streptococcal enzyme that acts specifically upon diphosphopyridine nucleotide: characterization of the enzyme and its separation from streptolysin O.J. Exp. Med. 106, 15–26 (1957).
Casida J.E., Augustinsson K.-B.: Reaction of plasma albumin with 1-naphthylN-methylcarbamate and certain other esters.Biochim. Biophys. Acta 36, 411–426 (1959).
Commoner B.: The biochemical basis of tobacco mosaic virus infectivity, pp. 17–30 in B.E. Frisch-Niggermeyer (Ed.):Proc. 4th Internat. Congr. Biochem. Vienna 1958. Symp. VII, Biochemistry of Viruses. Pergamon Press, London 1959.
Crawford I.P., Yanofsky C.: The formation of a new enzymatically active protein as a result of suppression.Proc. Nat. Acad. Sci. USA 45, 1280–1287 (1959).
Day P.R.: Genetics of recognition systems in host-parasite interactions, pp. 134–147 inEncyclopedia of Plant Physiology, New Series, Vol. 17. Springer-Verlag, Berlin 1984.
Dayhoff M.O.:Atlas of Protein Sequence and Structure 1972, Vol. 5. National Biomedical Research Foundation—Georgetown University Medical Center, Washington (DC) 1972.
Ellingboe A.H.: Changing concepts in host-pathogen genetics.Ann. Rev. Phytopathol. 19, 125–143 (1981).
Elsbach P., Pettis P.: Phospholipase activity associated with serum albumin.Biochim. Biophys. Acta 296, 89–93 (1973).
Fantl P.: Evolutionary trends in plasma mercaptalbumin composition.Comp. Biochem. Physiol. 42B, 403–408 (1972).
Fehrenbach F.J.: Gel-filtration behavior and molecular weight of NAD-glycohydrolase (EC 3.2.2.5) from streptococci in column chromatography on Sephadex gels.J. Chromatogr. 41, 43–52 (1969).
Flor H.H.: Current status of the gene-for-gene concept.Ann. Rev. Phytopathol. 9, 275–296 (1971).
Garen A.: Sense and nonsense in the genetic code.Science 160, 149–159 (1968).
Garen A., Siddiqi O.: Suppression of mutations in the alkaline phosphatase structural cistron ofE. coli.Proc. Nat. Acad. Sci. USA 48, 1121–1127 (1962).
Gooder H.: Antistreptolysin-O: its interaction with streptolysin O, its titration and a comparison of some standard preparations.Bull. WHO 25, 173–183 (1961).
Grlach D., Ozegowski J.H., Gunther E., Vettermann S., Kohler W.: Purification and some properties of streptococcal NAD-glycohydrolase.FEMS Microbiol. Lett. 136, 71–78 (1996).
Holland J.J.: Enterovirus entrance into specific host cells, subsequent alterations of cell protein and nucleic acid synthesis.Bacteriol. Rev. 28, 3–13 (1964).
Hooker A.H., Saxena K.M.S.: Genetics of disease resistance in plants.Ann. Rev. Genet. 5, 407–424 (1971).
Judah J.D., Gamble M., Steadman J.H.: Biosynthesis of serum albumin in rat liver. Evidence for the existence of proalbumin.Biochem. J. 134, 1083–1091 (1973).
Kameshita I., Matsuda Z., Taniguchi T., Shizuta Y.: Poly(ADP-ribose) synthetase.J. Biol. Chem. 259, 4770–4776 (1984).
Karush F.: Heterogeneity of the binding sites of bovine serum albumin.J. Am. Chem. Soc. 72, 2705–2718 (1950).
Kauzmann W., Simpson R.B.: The kinetics of protein denaturation. III. The optical rotations of serum albumin, β-lactoglobulin and pepsin in urea solutions.J. Am. Chem. Soc. 75, 5154–5157 (1953).
Knight C.A.: Purification of viruses: criteria of purity, pp. 25–29 inChemistry of Viruses, 2nd ed. Springer-Verlag, Wien-New York 1975.
Lauffer M.A., Stevens C.L.: Structure of the tobacco mosaic virus particle; polymerization of tobacco mosaic virus protein.Adv. Virus Res. 13, 1–63 (1968).
Lazarides P.D., Bernheimer A.W.: Association of production of diphosphopyridine nucleotidase with serological type of group AStreptococcus.J. Bacteriol. 74, 412–413 (1957).
Liu T.-Y., Neumann N.P., Elliott S.D., Moore S., Stein W.H.: Chemical properties of streptococcal proteinase and its zymogen.J. Biol. Chem. 238, 251–256 (1963).
Morgan F.J., Henschen A.: The structure of streptokinase I. Cyanogen bromide fragmentation, amino acid composition and partial amino acid sequences.Biochim. Biophys. Acta 181, 93–104 (1969).
Munk K., Schäfer W.: Eigenschaften tierischer Virusarten untersucht an den Geflügelpestviren als Modell—II. Mitteilung: Serologische Untersuchungen über die Geflügelpestviren und über ihre Beziehungen zu einem normalen Wirtsprotein.Z. Naturforsch. 6b, 372–379 (1951).
Nishizuka Y., Ueda K., Nakazawa K., Hayaishi O.: Studies on the polymer of adenosine diphosphate ribose—I. Enzymic formation from nicotinamide adenine dinucleotide in mammalian nuclei.J. Biol. Chem. 242, 3164–3171 (1967).
Pentz E.I., Kot E., Ferretti J.J.: Some characteristics of streptococcal nicotinamide adenine dinucleotidase and streptolysin O.J. Bacteriol. 88, 497–508 (1964).
Peters T. Jr.: Serum albumin, pp. 133–181 in F.W. Putnam (Ed.):The Plasma Proteins. Structure, Function and Genetic Control, Vol. 1. Academic Press, New York-San Francisco-London 1975.
Sigimura T., Miwa M.: Poly(ADP-ribose) and cancer research.Carcinogenesis 4, 1503–1506 (1983).
Stuart-Harris C.H., Schild G.C.: The molecular virology and replication of influenza viruses: morphology and chemical composition, pp. 23–27 inInfluenza. The Viruses and the Disease. Edward Arnold, London 1976.
Talal N., Hermann G., de Vaux S., Cyr C., Grabar P.: Immunoelectrophoretic study of mouse serum and urinary esterases. Chromatographic separation of albumin esterase.J. Immunol. 90, 246–256 (1963).
Tove S.B.: The esterolytic activity of serum albumin.Biochim. Biophys. Acta 57, 230–000 (1962).
Ueda K., Hayaishi O.: ADP-ribosylation.Ann. Rev. Biochem. 54, 73–100 (1985).
Williams G.T., Johnstone A.P.: ADP-ribosyl transferase, rearrangement of DNA, and cell differentiation.Biosci. Rep. 3, 815–830 (1983).
Wilson W.D., Foster J.F.: Conformation-dependent limited proteolysis of bovine plasma albumin by an enzyme present in commerical albumin preparations.Biochemistry 10, 1772–1780 (1971).
Zahradník F.J.: Streptococcal extracellular NAD-glycohydrolase. Optimal temperature and activation by cysteine.Folia Microbiol. 22, 92–97 (1977).
Zahradník F.J.: Streptococcal extracellular NAD+ nucleosidase. Characterization of changes occurring during purification.Folia Microbiol. 25, 40–49 (1980).
Žižkovský V., Štrop P., Lukešová Š., Korčáková J., Dvořák P.: Similarity of hydrophobic properties of α-fetoprotein and albumin.Oncodevelop. Biol. Med. 2, 323–330 (1981).
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Zahradník, F.J. Kinetic properties of fractions of extracellular NAD+ nucleosidase fromStreptococcus pyogenes as an example of host selection by a pathogen: Possible role of serum albumin in the organism. Folia Microbiol 46, 3–10 (2001). https://doi.org/10.1007/BF02825875
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DOI: https://doi.org/10.1007/BF02825875