Biopolym. Cell. 1994; 10(1):53-57.
http://dx.doi.org/10.7124/bc.000391
The role of nonenzymatic posttranslational deamidation and glycosylation process in aging of yeast cells Saccharomyces paradoxus
1Lukasch A. I., 1Puschkina N. V., 1Klimova I. A., 1Nasarova I. N.
  1. Institute biology
    Rostov State University
    194/1, Stachka Ave., Rostov-on-Don, Russian Federation, 344090

Abstract

The posttranslational nonenzymatic deamidation and glycosylation process in proteins from young and old yeast population cells were investigated. Yeast population Saccharomyces paradoxus were grown on minimal nitritional medium with 1, 2, 5, 10 % of glucose at 25 В°C. The in correlation between the rate of glycosylation and deamidation in cell proteins from yuong and old population was established. Posttranslational modifications of yeast cell proteins affected they were more actively by proteolytic enzymes.
Full text: (PDF, in Russian)

References

[1] Gillery P, Monboisse JC, Maquart FX, Borel JP. Aging mechanisms of proteins. Diabete Metab. 1991;17(1):1-16.
[2] Wright HT. Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit Rev Biochem Mol Biol. 1991;26(1):1-52.
[3] Appel N. Berich uber Symp. glykirte Hemoglobin Clin chem. 1987; 18(4):172-175.
[4] Dunn JA, Patrick JS, Thorpe SR, Baynes JW. Oxidation of glycated proteins: age-dependent accumulation of N epsilon-(carboxymethyl)lysine in lens proteins. Biochemistry. 1989;28(24):9464-8.
[5] Pushkina NV, Shepotinovskaia IV, Nazarov IP, Lukas AI. Role of non-enzymatic glycosylation of proteins accelerate the aging process. Accelerated aging: association with age pathology: Scientific. conf. Kyiv, 1992.
[6] Pushkina NV. Protein amidation in the aging organism. Ukr Biokhim Zh. 1979;51(6):680-3.
[7] Wlckerhau U. S. Jeast nitrogen base. Dep. A. G. Tech. Bull. 1951. N 1029: 2437-2465.
[8] Lyons S, Nelson N. An immunological method for detecting gene expression in yeast colonies. Proc Natl Acad Sci U S A. 1984;81(23):7426-30.
[9] Parker KM, England JD, Da Costa J, Hess RL, Goldstein DE. Improved colorimetric assay for glycosylated hemoglobin. Clin Chem. 1981;27(5):669-72.
[10] Pongor S, Ulrich PC, Bencsath FA, Cerami A. Aging of proteins: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose. Proc Natl Acad Sci U S A. 1984;81(9):2684-8.
[11] Shepotinovskaia IV. Effect of glutathione on the proteolytic degradation of tissue proteins in young and old rats. Ukr Biokhim Zh. 1986;58(4):14-8.
[12] Danilova LA, Fomenko MO, Leina LM. Glycation of proteins and methods of its assessment. Ukr Biokhim Zh. 1991;63(3):13-6.
[13] Azevedo MS. Maillard compounds as a cause of aging. Acta Med Port. 1990;3(2):126-8.
[14] Lowenson JD, Clarke S. Spontaneous degradation and enzymatic repair of aspartyl and asparaginyl residues in aging red cell proteins analyzed by computer simulation. Gerontology. 1991;37(1-3):128-51.
[15] Patel K, Borchardt RT. Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in a model hexapeptide. Pharm Res. 1990;7(7):703-11.
[16] Wright HT. Sequence and structure determinants of the nonenzymatic deamidation of asparagine and glutamine residues in proteins. Protein Eng. 1991;4(3):283-94.
[17] Tyler-Cross R, Schirch V. Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J Biol Chem. 1991;266(33):22549-56.
[18] Pushkina IV, Lukash AI. Easy and hard hydrolysable amide groups in protens. Izv. Severo-Kavkaz. nauch. tsentra vyssh. shk. yestestv. nauki. 1976-No 2: 95.
[19] Sharp JJ, Robinson AB, Kamen MD. Synthesis of a polypeptide with lysozyme activity. J Am Chem Soc. 1973;95(18):6097-108.