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. 1990 Jan;92(1):136–140. doi: 10.1104/pp.92.1.136

Variations in the Levels of Chloroplast tRNAs and Aminoacyl-tRNA Synthetases in Senescing Leaves of Phaseolus vulgaris1

Chelliah Jayabaskaran 1,2, Marcel Kuntz 1, Pierre Guillemaut 1, Jacques-Henry Weil 1
PMCID: PMC1062259  PMID: 16667235

Abstract

The relative amounts of chloroplast tRNAsLeu, tRNAGlu, tRNAPhe, tRNAsThr, and tRNATyr and of chloroplastic and cytoplasmic aminoacyl-tRNA synthetases were compared in green leaves, yellowing senescing leaves, and N6-benzyladenine-treated senescing leaves from bean (Phaseolus vulgaris, var Contender). Aminoacylation of the tRNAs using Escherichia coli aminoacyl-tRNA synthetases indicated that in senescing leaves the relative amount of chloroplast tRNAPhe was significantly lower than in green leaves. Senescing leaves treated with N6-benzyladenine contained higher levels of this tRNA than untreated senescing leaves. No significant change in the relative amounts of chloroplast tRNAsLeu, tRNAsThr, and tRNATyr was detected in green, yellow senescing, or N6-benzyladine-treated senescing leaves. Relative levels of chloroplast tRNAs were also estimated by hybridization of tRNAs to DNA blots of gene specific probes. These experiments confirmed the results obtained by aminoacylation and revealed in addition that the relative level of chloroplast tRNAGlu is higher in senescing leaves than in green leaves. Transcription run-on assays indicated that these changes in tRNA levels are likely to be due to a differential rate of degradation rather than to a differential rate of transcription of the tRNA genes. Chloroplastic and cytoplasmic leucyl-, phenylalanyl-, and tyrosyl-tRNA synthetase activities were greatly reduced in senescing leaves as compared to green leaves, whereas N6-benzyladenine-treated senescing leaves contained higher enzyme activities than untreated senescing leaves. These results suggest that during senescence, as well as during senescence-retardation by cytokinins, changes in enzyme activities, such as aminoacyl-tRNA synthetases, rather than reduced levels of tRNAs, affect the translational capacity of chloroplasts.

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Selected References

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  1. Amir-Shapira D., Goldschmidt E. E., Altman A. Chlorophyll catabolism in senescing plant tissues: In vivo breakdown intermediates suggest different degradative pathways for Citrus fruit and parsley leaves. Proc Natl Acad Sci U S A. 1987 Apr;84(7):1901–1905. doi: 10.1073/pnas.84.7.1901. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anderson M. B., Cherry J. H. Differences in leucyl-transfer rna's and synthetase in soybean seedlings. Proc Natl Acad Sci U S A. 1969 Jan;62(1):202–209. doi: 10.1073/pnas.62.1.202. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bick M. D., Liebke H., Cherry J. H., Strehler B. L. Changes in leucyl- and tyrosyl-tRNA of soybean cotyledons during plant growth. Biochim Biophys Acta. 1970 Mar 19;204(1):175–182. doi: 10.1016/0005-2787(70)90500-9. [DOI] [PubMed] [Google Scholar]
  4. Guillemaut P., Keith G. Primary structure of bean chloroplastic tRNAPhe. Comparison with Euglena chloroplastic tRNAPhe. FEBS Lett. 1977 Dec 15;84(2):351–356. doi: 10.1016/0014-5793(77)80723-0. [DOI] [PubMed] [Google Scholar]
  5. Herdenberger F., Weil J. H., Steinmetz A. Organization and nucleotide sequence of the broad bean chloroplast genes trnL-UAG, ndhF and two unidentified open reading frames. Curr Genet. 1988 Dec;14(6):609–615. doi: 10.1007/BF00434087. [DOI] [PubMed] [Google Scholar]
  6. Kuntz M., Weil J. H., Steinmetz A. Nucleotide sequence of a 2 kbp BamH I fragment of Vicia faba chloroplast DNA containing the genes for threonine, glutamic acid and tyrosine transfer RNAs. Nucleic Acids Res. 1984 Jun 25;12(12):5037–5047. doi: 10.1093/nar/12.12.5037. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lamattina L., Anchoverri V., Conde R. D., Lezica R. P. Quantification of the kinetin effect on protein synthesis and degradation in senescing wheat leaves. Plant Physiol. 1987 Mar;83(3):497–499. doi: 10.1104/pp.83.3.497. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Maréchal-Drouard L., Weil J. H., Guillemaut P. Import of several tRNAs from the cytoplasm into the mitochondria in bean Phaseolus vulgaris. Nucleic Acids Res. 1988 Jun 10;16(11):4777–4788. doi: 10.1093/nar/16.11.4777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Pfitzinger H., Guillemaut P., Weil J. H., Pillay D. T. Adjustment of the tRNA population to the codon usage in chloroplasts. Nucleic Acids Res. 1987 Feb 25;15(4):1377–1386. doi: 10.1093/nar/15.4.1377. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Schön A., Krupp G., Gough S., Berry-Lowe S., Kannangara C. G., Söll D. The RNA required in the first step of chlorophyll biosynthesis is a chloroplast glutamate tRNA. Nature. 1986 Jul 17;322(6076):281–284. doi: 10.1038/322281a0. [DOI] [PubMed] [Google Scholar]
  11. Silberklang M., Gillum A. M., RajBhandary U. L. Use of in vitro 32P labeling in the sequence analysis of nonradioactive tRNAs. Methods Enzymol. 1979;59:58–109. doi: 10.1016/0076-6879(79)59072-7. [DOI] [PubMed] [Google Scholar]
  12. Strehler B. L. The nature of cellular age changes. Symp Soc Exp Biol. 1967;21:149–177. [PubMed] [Google Scholar]
  13. Wright R. D., Pillay D. T., Cherry J. H. Changes in leucyl-tRNA species of pea leaves during senescence and after zeatin treatment. Mech Ageing Dev. 1973 Mar;1(5):403–412. doi: 10.1016/0047-6374(73)90046-8. [DOI] [PubMed] [Google Scholar]

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