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Lysine tRNAs from cytoplasm, chloroplasts and mitochondria of the lupin seedling cotyledons

Augustyniak, H.; Pawełkiewicz, J.

Acta Biochimica Polonica 25(1): 91-97

1978

ISSN/ISBN: 0001-527X
PMID: 665080
Document Number: 126146
1. The lupin cotyledons contain two cytoplasm-specific lysine tRNAs, one chloroplast-specific, one mitochondria-specific species, and three species common to all the cell compartments investigated; the lysine tRNAs were separated by reversed-phase chromatography (RPC-5). 2. The two cytoplasmic lysine tRNAs are predominant in the tRNALys isolated from the whole tissue. Their level and relative ratios change during germination (Augustyniak & Pawełkiewicz, 1978, Phytochemistry, 17, 15-18). 3. The organellar tRNA constitutes about 20% of the total tRNA in the cotyledons of 7-day-old lupin seedlings.

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Ivashchenko, A.T.; Karpeniuk, T.A.; Ponomarenko, S.V. 1991: ATP-synthase of bacteria, mitochondria, and chloroplasts. Properties of the F(0) membrane sector Biokhimiia 56(3): 406-419
Manson, J.C.; Liddell, A.D.; Leaver, C.J.; Murray, K. 1986: A protein specific to mitochondria from S-type male-sterile cytoplasm of maize is encoded by an episomal DNA EMBO Journal 5(11): 2775-2780
Mashanskiĭ, V.F.; Fridlianskaia, I.I.; Aksenova, N.N.; Brudnaia, M.S. 1973: Electron microscopic study of liver cell mitochondria, implanted in the cytoplasm of foreign cells Tsitologiia 15(10): 1203-1207
Ozerniuk, N.D.; Kotomin, A.V. 1978: Transfer of proteins synthesized in the cytoplasm into mitochondria. Stimulation of mitochondrial protein synthesis by microsomal fraction Biokhimiia 43(1): 67-71
Xue, J.-p.; Zhang, A.-m.; Sheng, W.; Zhang, G.-w. 2004: Comparative study on physiological and biochemical mechanism between virus-free seedling and common seedling in Chrysanthemum morifolium from Anhui Zhongguo Zhong Yao Za Zhi 29(6): 514-517
Hilbert, L.; Jenkins, P.V.; Gaucher, C.; Meriane, E.; Collins, P.W.; Pasi, K.J.; Mazurier, C. 2000: Type 2M vWD resulting from a lysine deletion within a four lysine residue repeat in the A1 loop of von Willebrand factor Thrombosis and Haemostasis 84(2): 188-194
Manangi, M.K.; Hoewing, S.F.A.; Engels, J.G.; Higgins, A.D.; Killefer, J.; Wilson, M.E.; Blemings, K.P. 2005: Lysine alpha-ketoglutarate reductase and lysine oxidation are distributed in the extrahepatic tissues of chickens Journal of Nutrition 135(1): 81-85
Tews, J.K.; Bradford, A.M.; Harper, A.E. 1981: Induction of lysine imbalance in rats: relation to competition for lysine transport into the brain in vitro Journal of Nutrition 111(6): 954-967
Ruklisha, M.P.; Ekabsone, M.A.; Viestur, U.E.; Mezhinia, G.R.; Selga, S.E. 1976: Regulation of growth and lysine-synthesizing activity of the lysine producer, Brevibacterium SP 22 L., by the intensity of stirring of the medium Prikladnaia Biokhimiia i Mikrobiologiia 12(4): 518-523
Lunts, M.G.; Gusiatiner, M.M.; Kopteva, A.V.; Zhdanova, N.I. 1986: Characteristics of lysine transport in a wild type strain and lysine-producing mutant of Corynebacterium glutamicum Prikladnaia Biokhimiia i Mikrobiologiia 22(1): 96-101
Marrs, T. 1996: Lupin-based food Health Bulletin 54(5): 366-367
Shen, W.C.; Ryser, H.J. 1979: Poly (L-lysine) and poly (D-lysine) conjugates of methotrexate: different inhibitory effect on drug resistant cells Molecular Pharmacology 16(2): 614-622
Madrzak, C.J.; Kulikova, O.; Legocki, A.B. 1989: Nodule-specific repression of yellow lupin protein R18 Acta Biochimica Polonica 36(3-4): 275-283
Schweizer, M.P.; Olsen, J.I.; De, N.; Messner, A.; Walkiw, I.; Grant, D.M. 1984: 13C NMR studies of dynamics and synthetase interaction of [4-13C]uracil-labeled Escherichia coli tRNAs Federation Proceedings 43(15): 2984-2986
Dalrymple, B.; Mattick, J.S. 1986: Genes encoding threonine tRNAs with the anticodon CGU from Escherichia coli and Pseudomonas aeruginosa Biochemistry International 13(4): 547-553
Tomaszewska, B.; Marczewski, W.; Schramm, R.W. 1983: Phosphoenolpyruvate carboxylase from the roots of yellow lupin (Lupinus luteus) Acta Biochimica Polonica 30(3-4): 265-275
Szweykowska-Kulińska, Z. 1992: Two intron-containing pre-tRNAs(Tyr) from Triticum aestivum are efficiently processed and spliced in homologous cell-free extract Acta Biochimica Polonica 39(3): 283-288
Hatfield, D.; Choi, I.S.; Mischke, S.; Owens, L.D. 1992: Selenocysteyl-tRNAs recognize UGA in Beta vulgaris, a higher plant, and in Gliocladium virens, a filamentous fungus Biochemical and Biophysical Research Communications 184(1): 254-259
Kiefer, S.; Greppin, H.; Penel, C. 1988: Association of a peroxidase to membranes of Pharbitis cotyledons Progress in Clinical and Biological Research 270: 289-290
Patykowski, J.; Urbanek, H.; Bytniewska, K. 1990: Changes in peroxidase activity in cell structures of lupin roots infected by Fusarium culmorum Acta Biochimica Polonica 37(2): 309-315