Summary
To extend the available information on the significance of the interactions between glycolytic enzymes and the actin component of the cellular ultrastructure, investigations into the compositional characteristics of the actin binding site on one of the major glycolytic enzymes, aldolase, have been undertaken. As the electrostatic nature of the association has been previously reported indicative of a cationic region on the enzyme involved in the binding, these studies have investigated the possibility of the involvement of histidine residues in this binding region. By the use of the histidine specific reagent, diethylpyrocarbonate, we have been able to establish a difference in nature of an actin binding domain and the active site domain which does contain an essential histidine. The results have been discussed in relation to the significance of this finding with respect to the binding of aldolase to subcellular structure.
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References
Masters CJ: Interactions between glycolytic enzymes and the cytomatrix. J Cell Biol 99:222–225, 1984
Clegg J: Properties and metabolism of the aqueous cytoplasm and its boundaries. Am J Physiol 246:R133-R151, 1984
Poglazov BF, Livanova NB: Interaction of actin with the enzymes of carbohydrate metabolism. Adv in Enz Regulation 25:297–305, 1985
Masters CJ, Reid S, Don M: Glycolysis — New concepts in an old pathway. Molecular and Cellular Biochemistry 76:3–14, 1987
Humphries L, Reid S, Masters CJ: Evidence for the spatial separation of the binding sites for substrate and for cytoskeletal proteins on the enzyme aldolase. Int J Biochem 18:7–13, 1986
Humphries L, Reid S, Masters CJ: Studies on the topographical localization of the binding sites for substrate and for actin on the enzymes, glyceraldehyde phosphate dehydrogenase and phosphofructokinase. Int J Biochem 18:445–451, 1986
Masters CJ: Interactions between soluble enzymes and subcellular structure. CRC Critical Reviews of Biochemistry 11:105–143, 1981
Lai CY: Studies on the Structure of Rabbit Muscle Aldolase. Determination of the primary structure of the COOH-Terminal BrCN peptide; the complete sequence of the subunit polypeptide chain. Arch Biochem Biophys 166:358–368, 1975
Melchior WB, Fahrney D: Ethoxyformylatin of proteins. Reaction of ethoxyformic anhydride with X chymotrypsin, pepsin and pancreatic ribonuclease at pH 4. Biochem 9:251–258, 1970
Baranowski T, Niederland TR: Aldolase activity of myogen A. J Biol Chem 180:543–535, 1949.
Walsh TP, Winzor DJ, Clarke FM, Masters CJ, Morton DJ: Binding of aldolase to actin containing filaments: Evidence of interaction with regulatory proteins of skeletal muscle. Biochem J 186:89–98, 1980
Ellman GL: Tissue Sulfhydryl Groups. Arch Biochem Biophys 82:70–77, 1959
Miles EW: Modification of histidyl residues in proteins with diethylpyrocarbonate. Methods in Enzymology 47:431–442, 1977
Ovadi J, Libor S, Elodi P: Spectrophotometric determination of histidine in proteins with diethylpyrocarbonate. Acta Biochim et Biophys Acad Sci Hung 2:445–458, 1967
Lundblad RL, Noyes CM: Modification of histidine residues. CRC Chemical Reagents for Protein Modification Vol 1, Chpt 9, 105–125, 1984
Smith GM, Mildvan AS: Nuclear magnetic resonance and chemical modification studies of the role of the metal in yeast aldolase. Biochemistry 20:4340–4346, 1981
Dominici P, Tancini B, Voltattorni CB: Chemical Modification of Pig Kidney 3,4 dihydroxyphenylalanine decarboxylase with diethylpyrocarbonate. J Biol Chem 260:10583–10589, 1985
Lai CY, Nakai N, Chang D: Amino acid sequence of rabbit muscle aldolase and structure of the active centre. Science 183:1204–1206, 1974
Hartman FC, Welch MH: Identification of the histidyl residue of rabbit muscle aldolase alkylated by N-bromoacetylethanolamine phosphate. Biochem Biophys Research Commun 57:85–92, 1974
Drechsler ER, Boyer PD, Kowalsky AG: The catalytic activity of carboxypeptidase-degraded aldolase. J Biol Chem 234:2627–2634, 1959
Rutter WJ, Richards OC, Woodfin BM: Comparative studies of liver and muscle aldolase. I. Effect of carboxypeptidase on catalytic activity. J Biol Cehm 236:3193–3197, 1961
Arnold H, Pette D: Binding of glycolytic enzymes to structure proteins of the muscle. Eur J Biochem 6:163–171, 1968
Murphy SM, Liu T, Kaul RK, Kohler H, Steck TL: The aldolase-binding site of the human erythrocyte membrane is at the NH2 terminus of band 3. J Biol Chem 256:11203–11208, 1981
Wilson JE: Ambiquitous enzymes; variation in intracellular distribution as a regulatory mechanism. Trends Biochem Sci 3:124–126, 1978
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Don, M., Masters, C. Chemical modification of the actin binding site of rabbit muscle aldolase by diethylpyrocarbonate. Mol Cell Biochem 81, 145–153 (1988). https://doi.org/10.1007/BF00219317
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DOI: https://doi.org/10.1007/BF00219317