Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1968 Sep;43(9):1355–1361. doi: 10.1104/pp.43.9.1355

Ribonuclease Activity Associated With Ribosomes of Zea mays 1

Theodore C Hsiao 1,2
PMCID: PMC1087021  PMID: 16656919

Abstract

At pH 6.5, a ribonuclease(s) is associated with ribosomes isolated from corn (Zea mays L.) and cannot be removed by repeated differential centrifugation or by sedimenting through the sucrose gradient. The enzyme is active under conditions favoring the maintenance of integrity of the ribosomes. Little or no latent ribonuclease appears to be present. The activity of the enzyme at pH 5.8 is stimulated by KCl and inhibited by polyvinyl sulfate, zinc, and bentonite. Deoxyribonuclease is also found on the particles.

The enzyme can be removed from ribosomes by adsorption onto bentonite. Ribosomes are also adsorbed but to a much lesser extent at low bentonite concentrations. The enzyme is easily dissociated from ribosomes by raising the pH to 8.5, and readsorbed when the pH is lowered.

The ribonuclease activity on ribosomes shows a sharp increase with cell age that parallels closely the increase in total activity in the homogenate. The ratio of activities of deoxyribonuclease to ribonuclease on ribosomes also changes with cell age and again the changes appear to reflect changes in the homogenate. It is suggested that most of the association of ribonuclease with corn ribosomes may not be meaningful in vivo and occurs only after the cells are ruptured.

Full text

PDF
1355

Images in this article

1356Image
on p.1356

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ARTMAN M., ENGELBERG H. DEGRADATION OF RAPIDLY-TURNED-OVER RIBONUCLEIC ACID TO ACID-SOLUBLE COMPOUNDS BY ESCHERICHIA COLI RIBOSOMES. Biochim Biophys Acta. 1964 Mar 23;80:517–520. doi: 10.1016/0926-6550(64)90158-6. [DOI] [PubMed] [Google Scholar]
  2. BONNER J., TS'O P. O., VINOGRAD J. Microsomal nucleoprotein particles from pea seedlings. J Biophys Biochem Cytol. 1956 Jul 25;2(4):451–466. doi: 10.1083/jcb.2.4.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. BROWNHILL T. J., JONES A. S., STACEY M. The inactivation of ribonuclease during the isolation of ribonucleic acids and ribonucleoproteins from yeast. Biochem J. 1959 Nov;73:434–438. doi: 10.1042/bj0730434. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. ELSON D. Latent enzymic activity of a ribonucleoprotein isolated from Escherichia coli. Biochim Biophys Acta. 1959 Dec;36:372–386. doi: 10.1016/0006-3002(59)90179-9. [DOI] [PubMed] [Google Scholar]
  5. FELLIG J., WILEY C. E. The inhibition of pancreatic ribonuclease by anionic polymers. Arch Biochem Biophys. 1959 Dec;85:313–316. doi: 10.1016/0003-9861(59)90496-5. [DOI] [PubMed] [Google Scholar]
  6. HSIAO T. C. CHARACTERISTICS OF RIBOSOMES ISOLATED FROM ROOTS OF ZEA MAYS. Biochim Biophys Acta. 1964 Dec 16;91:598–605. doi: 10.1016/0926-6550(64)90007-6. [DOI] [PubMed] [Google Scholar]
  7. KESSLER B., ENGELBERG N. Ribonucleic acid and ribonuclease activity in developing leaves. Biochim Biophys Acta. 1962 Jan 22;55:70–82. doi: 10.1016/0006-3002(62)90932-0. [DOI] [PubMed] [Google Scholar]
  8. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  9. Lyndon R. F. Intracellular distribution of ribonuclease activity in pea roots. Biochim Biophys Acta. 1966 Jan 11;113(1):110–119. doi: 10.1016/s0926-6593(66)80126-1. [DOI] [PubMed] [Google Scholar]
  10. NEU H. C., HEPPEL L. A. SOME OBSERVATIONS ON THE "LATENT" RIBONUCLEASE OF ESCHERICHIA COLI. Proc Natl Acad Sci U S A. 1964 Jun;51:1267–1274. doi: 10.1073/pnas.51.6.1267. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. OHTAKA Y., UCHIDA K. THE CHEMICAL STRUCTURE AND STABILITY OF YEAST RIBOSOMES. Biochim Biophys Acta. 1963 Sep 17;76:94–104. [PubMed] [Google Scholar]
  12. PETERMANN M. L., PAVLOVEC A. Ribonucleoprotein from a rat tumor, the Jensen sarcoma. II. Complexes formed with hemoglobin. J Biol Chem. 1961 Dec;236:3235–3239. [PubMed] [Google Scholar]
  13. PETERMANN M. L., PAVLOVEC A. Ribonucleoprotein from a rat tumor, the Jensen sarcoma. III. Ribosomes purified without deoxycholate but with bentonite as ribonuclease inhibitor. J Biol Chem. 1963 Jan;238:318–323. [PubMed] [Google Scholar]
  14. PIRIE N. W. The isolation from normal tobacco leaves of nucleoprotein with some similarity to plant viruses. Biochem J. 1950 Nov-Dec;47(5):614–625. doi: 10.1042/bj0470614. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. TAL M., ELSON D. THE LOCATION OF RIBONUCLEASE IN ESCHERICHIA COLI. Biochim Biophys Acta. 1963 Sep 17;76:40–47. [PubMed] [Google Scholar]
  16. TS'O P. O., BONNER J., VINOGRAD J. Structure and properties of microsomal nucleoprotein particles from pea seedlings. Biochim Biophys Acta. 1958 Dec;30(3):570–582. doi: 10.1016/0006-3002(58)90104-5. [DOI] [PubMed] [Google Scholar]
  17. WILSON C. M. Chromatographic separation of ribonucleases in corn. Biochim Biophys Acta. 1963 Feb 26;68:177–184. doi: 10.1016/0006-3002(63)90133-1. [DOI] [PubMed] [Google Scholar]
  18. WILSON C. M., SHANNON J. C. The distribution of ribonucleases in corn, cucumber, and soybean seedlings. Effects of isolation media. Biochim Biophys Acta. 1963 Feb 26;68:311–313. doi: 10.1016/0006-3002(63)90147-1. [DOI] [PubMed] [Google Scholar]
  19. WILSON C. M. SUBSTRATE AND PRODUCT SPECIFICITY OF TWO PLANT RIBONUCLEASES. Biochim Biophys Acta. 1963 Oct 15;76:324–326. [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES