Biopolym. Cell. 1996; 12(6):102-111.
Physicochemical properties of prosomes from leaves Datura stramonium L infected potato virus X
1Parkhomenko N. I., 1Didenko L. F., 1Maximenko L. A.
  1. D. K. Zabolotny Institute of Microbiology and Virology, NAS of Ukraine
    154, Academika Zabolotnogo Str., Kyiv, Ukraine, 03680


Low-molecular RNP or prosomes with sedimentation coefficient of 19 S and 10 S, which are being discovered only in cytoplasmatic mKNPs are absent in mRNP polysomes are isolated. The value of buoyant density of extracted structures in preformated gradient Cs2SO4 DMSO corresponds to 1,31 g/cm3 .On the basic of healthy and infected by potato virus X plants the protein composition of prosomes is defined. From prosomes preparation the low-molecular 4 S RNA is extracted.


[1] Arrigo AP, Tanaka K, Goldberg AL, Welch WJ. Identity of the 19S 'prosome' particle with the large multifunctional protease complex of mammalian cells (the proteasome). Nature. 1988;331(6152):192-4.
[2] Civelli O, Vincent A, Maundrell K, Buri JF, Scherrer K. The translational repression of globin mRNA in free cytoplasmic ribonucleoprotein complexes. Eur J Biochem. 1980;107(2):577-85.
[3] Schmid HP, Akhayat O, Martins De Sa C, Puvion F, Koehler K, Scherrer K. The prosome: an ubiquitous morphologically distinct RNP particle associated with repressed mRNPs and containing specific ScRNA and a characteristic set of proteins. EMBO J. 1984;3(1):29-34.
[4] Vincent A, Goldenberg S, Scherrer K. Comparisons of proteins associated with duck-globin mRNA and its polyadenylated segment in polyribosomal and repressed free messenger ribonucleoprotein complexes. Eur J Biochem. 1981;114(2):179-93.
[5] Jackson AO, Larkins BA. Influence of Ionic Strength, pH, and Chelation of Divalent Metals on Isolation of Polyribosomes from Tobacco Leaves. Plant Physiol. 1976;57(1):5-10.
[6] Ajtkhozhin MA, Akhanov AU. Release of mRNP-particles of the informosome type from polyribosomes of higher plant embryos. FEBS Lett. 1974;41(2):275-9.
[7] Takaiwa F, Tanifuji S. Relationship between translation-control and reduced polyadenylation of mRNA in elongated roots of pea seedlings. Plant and Cell Physiol. 1979; 20(5): 885-897.
[8] Dorokhov YuD, Aleksandrova NM, Miroshnichenko NA, Atabekov IG. Discovery of intracellular ribonucleiprotein particles during the infection of tobacco with a temperature sensitive mutant Ni118 of tobacco mosaic virus. Dokl vysh sh biol nauk. 1980; 6: 22-8.
[9] Greenberg JR. Isolation of messenger ribonucleoproteins in cesium sulfate density gradients: evidence that polyadenylated and non-polyadenylated messenger RNAs are associated with protein. J Mol Biol. 1976;108(2):403-16.
[10] Osterman LA. Methods of Protein and Nucleic Acid Research: Electrophoresis and ultracentrifugation. M.: Nauka. 1981; 288 p
[11] Belitsina NV, Ovchinnikov LP, Spirin AS, Ghendon JuZ, Chernos VI. Informosomes HeLa cells infected with vaccinia virus. Mol Biol (Mosk). 1968; (2):727-35.
[12] Shkipter VO. Methods of study of biopolymers by ultracentrifugation. Sovrem Metod biokhim. M, 1964. Vol1: 15-37.
[13] Practicum on general virology. Ed. IG Atabekova. Moscow: Moscow State University Press, 1981; (94-5) 192 p.
[14] As. N9 1451166. A method of determining the molecular mass heterogeneity of microbial polysaccharides. Votselko SL, Pirog TP, Malashenko YuR, Grinberg TA. Publ 1988.
[15] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976;72:248-54.
[16] Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(5259):680-5.
[17] Steele KP, Frist RH. Characterization of the 3' Termini of the RNAs of Cowpea Mosaic Virus. J Virol. 1978;26(2):243-8.
[18] Peacock AC, Dingman CW. Resolution of multiple ribonucleic acid species by polyacrylamide gel electrophoresis. Biochemistry. 1967;6(6):1818-27.
[19] Vincent A, Civelli O, Maundrell K, Scherrer K. Identification and characterization of the translationally repressed cytoplasmic globin messenger-ribonucleoprotein particles from duck erythroblasts. Eur J Biochem. 1980;112(3):617-33.
[20] Kremp A, Schliephacke M, Kull U, Schmid HP. Prosomes exist in plant cells too. Exp Cell Res. 1986;166(2):553-7.
[21] Ozaki M, Fujinami K, Tanaka K, Amemiya Y, Sato T, Ogura N, Nakagawa H. Purification and initial characterization of the proteasome from the higher plant Spinacia oleracea. J Biol Chem. 1992;267(30):21678-84.
[22] Dahlmann B, Kuehn L, Grziwa A, Zwickl P, Baumeister W. Biochemical properties of the proteasome from Thermoplasma acidophilum. Eur J Biochem. 1992;208(3):789-97.
[23] Sarkar S, Mukherjee AK, Guha C. A ribonuclease-resistant cytoplasmic 10 S ribonucleoprotein of chick embryonic muscle. A potent inhibitor of cell-free protein synthesis. J Biol Chem. 1981;256(10):5077-86.
[24] Mukherjee AK, Sarkar S. The translational inhibitor 10 S cytoplasmic ribonucleoprotein of chick embryonic muscle. Dissociation and reassociation. J Biol Chem. 1981;256(21):11301-6.
[25] Didenko LF, Maksimenko LA, Parkhomenko NI, Grabchenko NI, Kraev VG. Study of the composition of various-cell-location informosome in Datura stramonium plants infected with potato virus X. Mikrobiol Zh. 1989; 51(4):36-44.
[26] Didenko LF, Maksimenko LA, Parkhomenko NI. In vitro phosphorylation of informosome proteins from leaves of Stramonium infected with potato X-virus. Mikrobiol Zh. 1993; 55(2):68-74.
[27] Kraev VG, Didenko LF, Parkhomenko NI. Immunological analysis of mRNP proteins isolated from thorn apple leaves infected by popato virus X. Mikrobiol Zh. 1984;46(3):64-8.
[28] Parkhomenko NI, Didenko LF, Kraev VG. Relation of proteins to mRNA in mRNPs revealed in Datura stramonium leaves infected with popato virus X. Mikrobiol Zh. 1985; 47(6):61-4.
[29] Greenberg JR. The polyribosomal mRNA--protein complex is a dynamic structure. Proc Natl Acad Sci U S A. 1981;78(5):2923-6.
[30] Sonenberg N. ATP/Mg++-dependent cross-linking of cap binding proteins to the 5' end of eukaryotic mRNA. Nucleic Acids Res. 1981;9(7):1643-56.
[31] K?hn B, Villringer A, Falk H, Heinrich PC. Inhibition of cell-free protein synthesis by low-molecular-weight RNAs from free cytoplasmic ribonucleoprotein particles. Eur J Biochem. 1982;126(1):181-8.
[32] Horsch A, K?hler K, Ellwart-Tsch?rz M, Schmid HP. Selection of prosomes and prosomal RNA by immobilized viral RNAs. FEBS Lett. 1990;269(2):336-40.
[33] Horsch A, K?hler K, Schmid HP. Prosomes are involved in the repression of viral mRNA. Z Naturforsch C. 1985;40(5-6):449-50.