Treatment of Drosophila melanogaster Kc 0% cells with juvenile hormone (JH), which is of crucial importance to insect physiology, leads to a specific, early apparent increase in mitochondrial protein synthesis and to a later increase in cytochrome oxidase activity. This increase is at a maximum after a 12-h treatment with JH concentrations ranging from 10−12 to 10−9 M. Electrophoretic analysis of the mitochondrial translation products shows that all the mitochondria but a stimulating effect by a simultaneously. We saw no hormonal effect on isolated mitochondria but a stimulating effect by a post-mitochondrial supernatant from induced cells, strongly suggests that the action of JH is indirect and may result from a nuclear effect. 2-D electrophoretic analysis of the total mitochondrial proteins shows that at least two polypeptides coded by nuclear genome are affected. Such results suggest that despite the absence of morphological cellular modification, JH does have an active influence on energy metabolism.

Drosophila melanogaster mitochondrial DNA (mtDNA) is closely related to the mammalian and amphibian mtDNA except for gene organization. In Drosophila, genes are distributed in clusters alternatively coded on each strand. Besides the eleven major foreseeable transcripts previously described (MERTEN and PARDUE, 1981, J. Mol. Biol., 153, 1-21), we have characterized two poly A+ transcripts, one major and one minor which could correspond respectively to the ND3 and ND6 reading frames, and 27 poly A+ minor transcripts (0.2 to greater than 3.2 kb) which are distributed along the mtDNA except in the rRNAs, ND 1 and A+ T rich regions. The mapping and length of 25 of these transcripts strongly suggest a precursor role. They would be processed at the level of tRNA or tRNA-like sequences. Most of them are transcribed from the template strand of each gene cluster and their distribution is in agreement with the hypothesis of several transcription origins and terminations located near the extremities of each gene cluster. Quantitatively our results show a large variation in each presumptive mature transcript compared to the other, even in a given gene cluster, suggesting a specific degradation of some of the mature transcripts.

After osmotic shock with 50 mM Tricine buffer (pH 7.9), isolated mitochondria from D. Melanogaster embryos are treated with a low concentration of Triton X-100 (25 micrograms/mg of protein). The lysed mitochondria are still capable of RNA and protein synthesis. While incorporation of labeled precursor is often higher in lysed than in intact mitochondria, neosynthesized proteins exhibit similar electrophoretic patterns. Studies of labeled precursor incorporation in the presence of various effectors indicate a better accessibility to the translation machinery in lysed mitochondria than in intact mitochondria. Such a system has proven capable of translating an exogenous synthetic mRNA, i.e., poly (U).

L'expression du génome mitochondrial de D. melanogaster est étudiée par incorporation de méthionine 35S dans des mitochondries isolées d'embryons précoces.

Myofibrillar ATPase activity (in the presence of Ca2+ and Mg2+), activities of various glycolytic and mitochondrial enzymes, and haemin iron, glycogen, ATP and lactic acid levels were determined in the heart and five skeletal muscles of the sheep as a function of age and sex. During growth from 2 to 13 months, ATPase activity remained stable whereas most mitochondrial and glycolytic activities tended to decrease, particularly betwen 2 and 6 months. The isoenzyme composition of lactic dehydrogenase evolued markedly, with in particular a rise in the percentage of M4. Haemin iron level rose from 6 months. These modifiations occurred in most of the skeletal muscles but rarely in the heart. Glycogen and ATP decreased progressively between 2 and 13 months. Overall, results indicated a regression of the metabolic differentiation among muscles between 2 and 13 months, particularly marked before 6 months. At 3 and 7 months, sex had practically no influence on the enzyme activities studied.

The metabolic characteristics of 12 skeletal muscles of the sheep were studied.

Adenine nucleotide transport and the influx of inorganic phosphate into mitochondria are directly linked to intramitochondrial ATP synthesis. Much work has been done on the isolation of the adenine-nucleotide translocase and the reconstitution of its transport system. The present state of research into the proteins involved in phosphate transport is described.

FEBS LettersVolume 128, Issue 1 p. 142-144 Full-length articleFree Access Purification of a phosphate carrier in pig heart mitochondria by affinity chromatography on mersalyl—ultrogel Sylvie Touraille, Sylvie Touraille Laboratoire de Biochimie, ERA 692, Université de Clermont II, B.P. 45, 63170 Aubiere, FranceSearch for more papers by this authorYves Briand, Yves Briand Laboratoire de Biochimie, ERA 692, Université de Clermont II, B.P. 45, 63170 Aubiere, FranceSearch for more papers by this authorRogert Durand, Corresponding Author Rogert Durand Laboratoire de Biochimie, ERA 692, Université de Clermont II, B.P. 45, 63170 Aubiere, FranceTo whom reprint requests should be addressedSearch for more papers by this authorJean-Claude Bonnafous, Jean-Claude Bonnafous Laboratoire de Biochimie des Membranes, ERA 228, 8, rue de l'Ecole Normale, 34075 Montpellier, FranceSearch for more papers by this authorJean-Claude Mani, Jean-Claude Mani Laboratoire de Biochimie des Membranes, ERA 228, 8, rue de l'Ecole Normale, 34075 Montpellier, FranceSearch for more papers by this author Sylvie Touraille, Sylvie Touraille Laboratoire de Biochimie, ERA 692, Université de Clermont II, B.P. 45, 63170 Aubiere, FranceSearch for more papers by this authorYves Briand, Yves Briand Laboratoire de Biochimie, ERA 692, Université de Clermont II, B.P. 45, 63170 Aubiere, FranceSearch for more papers by this authorRogert Durand, Corresponding Author Rogert Durand Laboratoire de Biochimie, ERA 692, Université de Clermont II, B.P. 45, 63170 Aubiere, FranceTo whom reprint requests should be addressedSearch for more papers by this authorJean-Claude Bonnafous, Jean-Claude Bonnafous Laboratoire de Biochimie des Membranes, ERA 228, 8, rue de l'Ecole Normale, 34075 Montpellier, FranceSearch for more papers by this authorJean-Claude Mani, Jean-Claude Mani Laboratoire de Biochimie des Membranes, ERA 228, 8, rue de l'Ecole Normale, 34075 Montpellier, FranceSearch for more papers by this author First published: June 01, 1981 https://doi.org/10.1016/0014-5793(81)81100-3Citations: 19AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat No abstract is available for this article.Citing Literature Volume128, Issue1June 01, 1981Pages 142-144 ReferencesRelatedInformation

In order to study the interrelation between nuclear genome and mitochondria during biogenesis of mitochondrial proteins, mitochondria of D. melanogaster were isolated from whole insects.

Lactate dehydrogenase activity and isoenzyme distribution were measured in fast-twitch red, slow-twitch red and fast-twitch white muscles in the sheep. Total enzyme activity is higher in fast-twitch muscles irrespective of their colour type. Isoenzymes M4 and H4 bear an inverse relationship, M4 being predominant in fast-twitch red and white muscles, and H4 in heart muscle and slow-twitch red muscles.

FEBS LettersVolume 121, Issue 2 p. 230-234 Full-length articleFree Access Discrimination between the N-ethylmaleimide mersalyl-sensitive protein(s) and the nucleotide translocator in pig heart mitochondria Sylvie Touraille, Sylvie Touraille Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorYves Briand, Yves Briand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorSerge Alziari, Serge Alziari Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorRoger Durand, Roger Durand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this author Sylvie Touraille, Sylvie Touraille Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorYves Briand, Yves Briand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorSerge Alziari, Serge Alziari Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorRoger Durand, Roger Durand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this author First published: December 01, 1980 https://doi.org/10.1016/0014-5793(80)80349-8Citations: 10AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinked InRedditWechat Citing Literature Volume121, Issue2December 01, 1980Pages 230-234 ReferencesRelatedInformation

Opening of the terminal hemi-acetal in dihydronigericin drastically reduces the ionophoric properties of nigericin and dehydroxymethylnigericin with 6 intact heterocycles. This is shown by 2 complementary methods, first with a liquid membrane electrode system, secondly by testing their ionophoric activities in rat liver mitochondria.

The alkali cations discrimination on a liquid membrane electrodes system, was determined for the carboxylic ionophores grisorixin, alborixin and two derivatives, dihydrogrisorixin and hexahydroalborixin. The two antibiotics exhibited a great perference for K+. Dihydrogrisorixin again showed the selectivity curve of a carboxylic ionophore, but with a discrimination power lowered compared with grisorixin. Hexahydroalborixin had lost all the complexing properties of the natural molecule. The selectivity scales measured for cations, were directly correlated with the K+ and glutamate effluxes measured in rat liver mitochondria. The chemical modifications of the natural structures of grisorixin and alborixin resulted in a drastic reduction of their ionophoric properties. The loss of K+-glutamate might occur in two steps, the efflux of K+ catalysed by the ionophores then causing a loss of negative charges in the form of glutamate.

Phosphate transport in rat liver mitochondria was studied by following [32P] phosphate uptake within physiological concentrations. Transport inhibition due to mersalyl and protection by mersalyl against N-ethylmaleimide measured in those conditions corresponded to earlier results obtained by the swelling technique. When mitochondria were incubated with [3H] N-ethylmaleimide in the presence of mersalyl, the radioactive labeling in proteins of particles obtained after sonication was decreased in all fractions, but three proteins were both highly alkylated and also highly protected by mersalyl (M.W. 48,000 - 36,000 - 31,000). Two of these (M.W. 36,000 and 31,000) were partially purified by ultrogel chromatography in the presence of sodium dodecyl sulfate. Furthermore, it was shown that both phosphate and nigericin diminished labeling by N-ethylmaleimide in the final supernatant fraction. Two proteins (M.W. 98,000 and 31,000) were significantly alkylated by [3H] N-ethylmaleimide and protected by phosphate and nigericin.

FEBS LettersVolume 85, Issue 2 p. 321-325 Full-length articleFree Access Inhibition by pyruvate of pig heart mitochondrial glutamate influx Georges Stepien, Georges Stepien Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorRoger Debise, Roger Debise Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorRoger Durand, Corresponding Author Roger Durand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceTo whom reprint requests should be addressedSearch for more papers by this author Georges Stepien, Georges Stepien Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorRoger Debise, Roger Debise Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorRoger Durand, Corresponding Author Roger Durand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceTo whom reprint requests should be addressedSearch for more papers by this author First published: January 15, 1978 https://doi.org/10.1016/0014-5793(78)80483-9Citations: 1AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 A.L. Lehninger, H.C. Sudduth, J.B. Wise, J. Biol. Chem., 235, (1960), 2450– 2455. 2 J.L Purvis, J.M. Lowenstein, J. Biol. Chem., 236, (1961), 2794– 2803. 3 P. Borst, P. Karlson Functionelle und morphologische Organisation der Zell (1963), Springer-Verlag Berlin 137– 158. 4 J.R. Williamson, B. Safer, K.F. Lanoue, C.M. Smith, E. Walajtys, Symp. Soc. Exp. Biol., 27, (1973), 241– 281. 5 K.F. LaNoue, M.E. Tischler, J. Biol. Chem., 249, (1974), 7522– 7528. 6 J.H. Julliard, D.C. Gautheron, FEBS Lett., 37, (1973), 10– 16. 7 E.C. Slater, C. Tamblyn-Hague, Thiene D. Van, Biochim. Biophys. Acta, 96, (1965), 206– 216. 8 E.J. Davis, Biochim. Biophys. Acta, 96, (1965), 217– 230. 9 A. Younes, R. Durand, Y. Briand, D.C. Gautheron, Bull. Soc. Chim. Biol., 52, (1970), 811– 830. 10 F.L. Crane, J.F. Gleen, D.E. Green, Biochim. Biophys. Acta, 22, (1956), 476– 11 A.G. Gornall, L.J. Bardawill, M.M. David, J. Biol. Chem., 177, (1949), 751– 766. 12 J. Meyer, P.M. Vignais, Biochim. Biophys. Acta, 325, (1973), 375– 394. 13 N.M. Bradford, J.D. McGivan, Biochem. J., 134, (1973), 1023– 1029. 14 K.F. LaNoue, J. Bryla, D.J.P. Bassett, J. Biol. Chem., 249, (1974), 7514– 7521. 15 J.M. Haslam, H.A. Krebs, Biochem. J., 107, (1968), 659– 667. 16 F. Passarella, F. Palmieri, E. Quagliariello, Arch. Biochem. Biophys., 180, (1977), 160– 168. 17 D.L. Severson, R.M. Denton, H.T. Pask, P.J. Randle, Biochem. J., 140, (1974), 225– 237. 18 R. Rognstad, J. Katz, Biochem. J., 116, (1970), 483– 491. Citing Literature Volume85, Issue2January 15, 1978Pages 321-325 ReferencesRelatedInformation

FEBS LettersVolume 85, Issue 1 p. 25-29 Full-length articleFree Access Correlation between glutamate and Ca2+ uptake in rat liver mitochondria Roger Debise, Roger Debise Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorPierre Gachon, Pierre Gachon Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, France Laboratoire de Pharmacologie Médicale, Formation de Recherche Associée à l'INSERM No. 10, UER de Médecine, 63001 Clermont-Ferrand-Cedex, FranceSearch for more papers by this authorRoger Durand, Corresponding Author Roger Durand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceTo whom reprint requests should be addressedSearch for more papers by this author Roger Debise, Roger Debise Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceSearch for more papers by this authorPierre Gachon, Pierre Gachon Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, France Laboratoire de Pharmacologie Médicale, Formation de Recherche Associée à l'INSERM No. 10, UER de Médecine, 63001 Clermont-Ferrand-Cedex, FranceSearch for more papers by this authorRoger Durand, Corresponding Author Roger Durand Laboratoire de Biochimie, Université de Clermont-Ferrand II, BP 45, 63170 Aubière, FranceTo whom reprint requests should be addressedSearch for more papers by this author First published: January 01, 1978 https://doi.org/10.1016/0014-5793(78)81240-XCitations: 5AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 J.B. Chappel, M. Cohin, G.D. Greville, B. Chance Energy Linked Functions of Mitochondria (1963), Academic Press 219– 231. 2 B. Chance, J. Biol. Chem., 240, (1965), 2729– 2748. 3 C.S. Rossi, J. Bielawski, A.L. Lehninger, J. Biol. Chem., 241, (1966), 1919– 1921. 4 A.L. Lehninger, Proc. Natl. Acad. Sci. USA, 71, (1974), 1520– 1524. 5 H. Rottenberg, A. Sc??pa, Biochemistry, 13, (1974), 4811– 4817. 6 B. Reynafarje, A.L. Lehninger, Biochem. Biophys. Res. Commun., 77, (1977), 1273– 1279. 7 J. Moyle, P. Mitchell, FEBS Lett., 73, (1977), 131– 136. 8 A. Azzi, J.B. Chappell, B.H. Robinson, Biochem. Biophys. Res. Commun., 29, (1867), 148– 152. 9 Noue K.F. La, M.E. Tischler, J. Biol. Chem., 249, (1974), 7522– 7528. 10 Noue K.F. La, A.J. Meijor, A. Brouwer, Arch. Biochem. Biophys., 161, (1974), 544– 550. 11 A.S. Meijer, A. Brouwer, D.J. Reijngoud, J.B. Hoek, J.M. Tager, Biochem. Biophys. Acta, 283, (1972), 421– 429. 12 J. Meyer, P.M. Vignais, Biochim. Biophys. Acta, 325, (1973), 375– 394. 13 N.M. Bradford, Givan J.D. Mc, Biochem. J., 134, (1973), 1023– 1029. 14 R. Debise, R. Durand, Biochimie, 56, (1974), 161– 170. 15 J.B. Hoek, R.M. Njogu, FEBS Lett., 71, (1976), 341– 346. 16 D. Johnson, H.A. Lardy, Methods in enzymology X, (1967), Academic Press 94– 96. 17 A.G. Gornall, L.H. Bardawill, M.M. David, J. Biol. Chem., 177, (1949), 751– 766. 18 R. Debise, Y. Briand, R. Durand, P. Gachon, G. Jeminet, Biochimie, 59, (1977), 497– 508. 19 D. Ammonn, M. Giuggi, E. Pretsch, W. Simon, Anal. Lett., 8, (1975), 705– 720. 20 P. Mitchell, J. Moyle, Eur. J. Biochem., 7, (1969), 471– 484. 21 E. Padan, H. Rottenberg, Eur. J. Biochem., 40, (1973), 431– 437. 22 P. Mitchell, J. Moyle, Eur. J. Biochem., 9, (1969), 149– 155. 23 F. Palmieri, E. Quagliariello, M. Klingenberg, Eur. J. Biochem., 17, (1970), 230– 238. Citing Literature Volume85, Issue1January 01, 1978Pages 25-29 ReferencesRelatedInformation