From polynucleotide phosphorylase to neurobiology

Journal of Biological Chemistry

Volumn 280, Issue 47, 2005, Pages 38889-38897

  Littauer, Uriel Z ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; DNA; GLOBIN; POLYRIBONUCLEOTIDE; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; RIBOSOME RNA; RNA; TRANSFER RNA;

BIOCHEMISTRY; CAREER; EMPLOYMENT; ENZYME ACTIVITY; ENZYME ANALYSIS; HUMAN; JOB FINDING; MEDICAL EDUCATION; MEDICAL RESEARCH; MOLECULAR BIOLOGY; NEUROBIOLOGY; POSTGRADUATE EDUCATION; PRIORITY JOURNAL; REVIEW; RNA SYNTHESIS;

ANIMALS; AUTOBIOGRAPHY; HISTORY, 20TH CENTURY; HISTORY, 21ST CENTURY; HUMANS; ISRAEL; NEUROBIOLOGY; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; RNA; UNITED STATES;

EID: 28244432495     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/JBC.X500007200     Document Type: Review

References (70)

1. Ginsburg, D. (1963) Ernst David Bergmann, an appreciation on the occasion of , his sixtieth birthday. Isr. J. Chem. 1, 323-350
2. Grunberg-Manago, M., Ortiz, P. J., and Ochoa, S. (1956) Enzymic synthesis of polynucleotides. I. Polynucleotide phosphorylase of Azotobacter vinelandii. Biochim. Biophys. Acta 20, 269 -285
3. Littauer, U. Z., and Kornberg, A. (1957) Reversible synthesis of polyribonucleotides with an enzyme from Escherichia coli. J. Biol. Chem. 226, 1077-1092
4. Littauer, U. Z., and Soreq, H. 1982. Polynucleotide phosphorylase. In The Enzyme (Boyer, P. D., ed) Vol. 15, pp. 517-553, Academic Press, New York
5. Littauer, U. Z., and Grunberg-Manago, M. (1999) Polynucleotide phosphorylase. In Encyclopedia of Molecular Biology (Creighton, T. E., ed) Vol. 3, pp. 1911-1918, John Wiley and Sons, New York
6. Kimhi, Y., and Littauer, U. Z. (1968) Purification and properties of polynucleotide phosphorylase from Escherichia coli J. Biol. Chem. 243, 231-240
7. Leder, P., Singer, M. F., and Brimacombe, R. L. (1965) Synthesis of trinucleoside diphosphates with polynucleotide phosphorylase. Biochemistry 4, 1561-1567
8. Moses, R. E., and Singer, M. F. (1970) Polynucleotide phosphorylase of Micrococcus luteus. Studies on the polymerization reaction catalyzed by primer-dependent and primer-independent enzymes. J. Biol. Chem. 245, 2414-2422
9. Littauer, U. Z., and Eisenberg, H. (1959) Ribonucleic acid from Escherichia coli preparation, characterization and physical properties. Biochim. Biophys. Acta 32, 320-337
10. Littauer, U. Z. (2000) The unfolding of our understanding of RNA structure: a personal reflection. Biophys. Chem. 86, 259-266
11. Rich, A., and Watson, I. D. (1954) Physical studies on ribonucleic acid. Nature 173, 995-996
12. Littauer, U. Z. (2003) RNA enzymology and beyond. In Comprehensive Biochemistry (Semenza, G., and Turner, A. J., eds) Vol. 42, pp. 221-284, Elsevier Science Publishers E.V., Amsterdam
13. Daniel, V, Sarid, S., and Littauer, U. Z. (1970) Bacteriophage induced transfer RNA in Escherichia coli. New transfer RNA molecules are synthesized on the bacteriophage genome. Science 167, 1682-1688
14. Daniel, V., Beckmann, J. S., Sarid, S., Grimberg, J. I., Herzberg, M., and Littauer, U. Z. (1971) Purification and in vitro transcription of a transfer RNA gene. Proc. Natl. Acad. Sci. U. S. A. 68, 2268-2272
15. Kimhi, Y., and Littauer, U. Z. (1967) The intracellular distribution of polynucleotide phosphorylase in Escherichia coli cells. Biochemistry 6, 2066-2073
16. Soreq, H., and Littauer, U. Z. (1977) Purification and characterization of polynucleotide phosphorylase from Escherichia coli. Probe for the analysis of 3′ sequences of RNA. J. Biol. Chem. 252, 6885-6888
17. Soreq, H., Nudel, U., Salomon, R., Revel, M., and Littauer, U. Z. (1974) In vitro translation of polyadenylic acid-free rabbit globin messenger RNA. J. Mol. Biol. 88, 233-245
18. Huez, G., Marbaix, G., Hubert, E., Leclercq, M., Nudel, U., Soreq, H., Salomom, R., Lebleu, B., Revel, M., and Littauer, U. Z. (1974) Role of the polyadenylate segment in the translation of globin messenger RNA in Xenopus oocytes. Proc. Natl. Acad. Sci. U. S. A. 71, 3143-3146
19. Littauer, U. Z., and Soreq, H. (1982) The regulatory function of poly(A) and adjacent 3′ sequences in translated RNA. Prog. Nucleic Acids Res. Mol. Biol. 27, 53-83
20. Nudel, U., Soreq, H., Littauer, U. Z., Marbaix, G., Huez, G., Leclercq, M., Hubert, E., and Chantrenne, H. (1976) Globin mRNA species containing poly(A) segments of different lengths. Their functional stability in Xenopus oocytes. Eur. J. Biochem. 64, 115-121
21. Baer, B. W., and Kornberg, R. D. (1983) The protein responsible for the repeating structure of cytoplasmic poly(A)-ribonucleoprotein. J. Cell Biol. 96, 717-721
22. Littauer, U. Z. (1993) Co-chairman's remarks: reflections on RNA. Gene (Amst.) 135, 209-214
23. Deo, R. C., Bonanno, I. B., Sonenberg, N., and Burley, S. K. (1999) Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell 98, 835-845
24. Grosfeld, H., Soreq, H., and Littauer, U. Z. (1977) Membrane associated cytoplasmic mRNA in Artemia salina; functional and physical changes during development. Nucleic Acids Res. 4, 2109-2121
25. Salomon, R., Sela, I., Soreq, H., Giveon, D., and Littauer, U. Z. (1976) Enzymatic acylation of histidine to tobacco mosaic virus RNA. Virology 71, 74-84
26. Kaufmann, G., Grosfeld, H., and Littauer, U. Z. ( 1973) Stepwise phosphorolysis with polynucleotide phosphorylse: a novel method for sequence analysis of oligoribonucleotides. FEBS Lett. 31, 47-52
27. Kaufmann, G., and Littauer, U. Z. (1969) Deoxyadenosine diphosphate as substrate for polynucleotide phosphorylase from Escherichia coli. FEBS Lett. 4, 79-83
28. Kaufmann, G., and Littauer, U. Z. (1970) Phosphorolysis of aminoacyl-tRNA by polynucleotide phosphorylase from Escherichia coli. Eur. J. Biochem. 12, 85-92
29. Kaufmann, G., Fridkin, M., Zutra, A., and Littauer, U. Z. (1971) Monofunctional substrates of polynucleotide phosphorylase. The monoaddition of 2′(3′)-isovaleryl-nucleoside diphosphate to an initiator oligonucleotide. Eur. J. Biochem. 24, 4-11
30. Kaufmann, G., and Littauer, U. Z. (1974) Covalent joining of phenylalanine transfer ribonucleic acid half-molecules by T4 RNA ligase. Proc. Natl. Acad. Sci. U. S. A. 71, 3741-3745
31. old-35, in the context of terminal differentiation and cellular senescence. Proc. Natl. Acad. Sci. U. S. A. 99, 16636-16641
32. Leszczyniecka, M., DeSalle, R., Kang, D. C., and Fisher, P. B. (2004) The origin of polynucleotide phosphorylase domains. Mol. Phylogenet. Evol. 31, 123-130
33. old-35): a potential link between aging and inflammation. Cancer Res. 64, 7473-7478
34. Piwowarski, J., Grzechnik, P., Dziembowski, A., Dmochowska, A., Minczuk, M., and Stepien, P. P. (2003) Human polynucleotide phosphorylase, hPNPase, is localized in mitochondria. J. Mol. Biol. 329, 853-857
35. Raijmakers, R., Egberts, W. V., van Venrooij, W. J., and Pruijn, G. J. (2002) Protein-protein interactions between human exosome components support the assembly of RNase PH-type subunits into a six-membered PNPase-like ring. J. Mol. Biol. 323, 653-663
36. Baginsky, S., Shteiman-Kotler, A., Liveanu, V., Yehudai-Resheff, S., Bellaoui, M., Settlage, R. E., Shabanowitz, J., Hunt, D. F., Schuster, G., and Gruissem, W. (2001) Chloroplast PNPase exists as a homo-multimer enzyme complex that is distinct from the Escherichia coli degradosome. RNA 7, 1464-1475
37. Yehudai-Resheff, S., Portnoy, V., Yogev, S., Adir, N., and Schuster, G. (2003) Domain analysis of the chloroplast polynucleotide phosphorylase reveals discrete functions in RNA degradation, polyadenylation, and sequence homology with exosome proteins. Plant Cell 15, 2003-2019
38. Portier, C. (1975) Quaternary structure of polynucleotide phosphorylase from Escherichia coli: evidence of a complex between two types of polypeptide chains. Eur. J. Biochem. 55, 573-582
39. Régnier, P., Grunberg-Manago, M., and Portier, C. (1987) Nucleotide sequence of the pnp gene of Escherichia coli encoding polynucleotide phosphorylase. Homology of the primary structure of the protein with the RNA-binding domain of ribosomal protein S1. J. Biol. Chem. 262, 63-68
40. Mathy, N., Jarrige, A. C., Robert-Le Meur, M., and Portier, C. (2001) Increased expression of Escherichia coli polynucleotide phosphorylase at low temperatures is linked to a decrease in the efficiency of autocontrol. J. Bacteriol. 183, 3848-3854
41. Jarrige, A. C., Mathy, N., and Portier, C. (2001) PNPase autocontrols its expression by degrading a double-stranded structure in the pnp mRNA leader. EMBO J. 20, 6845-6855
42. Symmons, M. F., Jones, G. H., and Luisi, B. F. (2000) A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation. Structure 8, 1215-1226
43. Symmons, M. F., Williams, M. G., Luisi, B. F., Jones, G. H., and Carpousis, A. J. (2002) Running rings around RNA: a superfamily of phosphate-dependent RNases. Trends Biochem. Sci. 27, 11-18
44. Zuo, Y., and Deutscher, M. P. (2001) Exoribonuclease superfamilies: structural analysis and phylogenetic distribution. Nucleic Acids Res. 29, 1017-1026
45. Donovan, W. P., and Kushner, S. R. (1986) Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Proc. Natl. Acad. Sci. U. S. A. 83, 120-124
46. Li, Z., Reimers, S., Pandit, S., and Deutscher, M. P. (2002) RNA quality control: degradation of defective transfer RNA. EMBO J. 21, 1132-1138
47. Kelly, K. O., and Deutscher, M. P. (1992) Characterization of Escherichia coli RNase PH. J. Biol. Chem. 267, 17153-17158
48. Harlow, L. S., Kadziola, A., Jensen, K. F., and Larsen, S. (2004) Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis and implications for its quaternary structure and tRNA binding. Protein Sci. 13, 668-677
49. Valentine, R. C., Thang, M. N., and Grunberg-Manago, M. (1969) Electron microscopy of Escherichia coli polynucleotide phosphorylase molecules and polyribonucleotide formation. J. Mol. Biol. 39, 389-391
50. Jones, G. H., and Bibb, M. J. (1996) Guanosine pentaphosphate synthetase from Streptomyces antibioticus is also a polynucleotide phosphorylase. J. Bacteriol. 178, 4281-4288
51. Bralley, P., and Jones, G. H. (2004) Organization and expression of the polynucleotide phosphorylase gene (pnp) of Streptomyces: processing of pnp transcripts in Streptomyces antibioticus. J. Bacteriol. 186, 3160-3172
52. Kushner, S. R. (2002) mRNA decay in Escherichia coli comes of age. J. Bacteriol. 184, 4658-4665
53. Carpousis, A. J., Vanzo, N. F., and Raynal, L. C. (1999) mRNA degradation. A tale of poly(A) and multiprotein machines. Trends Genet. 15, 24-28
54. Khemici, V., and Carpousis, A. J. (2004) The RNA degradosome and poly(A) polymerase of Escherichia coli are required in vivo for the degradation of small mRNA decay intermediates containing REP-stabilizers. Mol. Microbiol. 51, 777-790
55. Bernstein, J. A., Lin, P. H., Cohen, S. N., and Lin-Chao, S. (2004) Global analysis of Escherichia coli RNA degradosome function using DNA microarrays. Proc. Natl. Acad. Sci. U. S. A. 101, 2758-2763
56. Ow, M. C., Liu, Q., and Kushner, S. R. (2000) Analysis of mRNA decay and rRNA processing in Escherichia coli in the absence of RNase E-based degradosome assembly. Mol. Microbiol. 38, 854-866
57. Mohanty, B. K., and Kushner, S. R. (2000) Polynucleotide phosphorylase functions both as a 3′-5′ exonuclease and a poly(A) polymerase in Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 97, 11966-11971
58. Schrier, B. K., Wilson, S. H., and Nirenberg, M. (1974) Cultured cell systems and methods for neurobiology. Methods Enzymol. 32, 765-788
59. Littauer, U. Z., Giovanni, M., and Glick, M. C. (1980) Glycoprotein from neurite of differentiated neuroblastoma cells. J. Biol. Chem. 255, 5448-5453
60. Kimhi, Y., Palfrey, C., Spector, I., Barak, Y., and Littauer, U. Z. (1976) Maturation of neuroblastoma cells in the presence of dimethylsulfoxide. Proc. Natl. Acad. Sci. U. S. A. 73, 462- 466
61. Soreq, H., Miskin, R., Zutra, A., and Littauer, U. Z. (1983) Modulation in the levels and localization of plasminogen activator in differentiating neuroblastoma cells. Dev. Brain Res. 7, 257-269
62. Periz, G., and Fortini, M. E. (2000) Proteolysis in Alzheimer's disease. Can plasmin tip the balance? EMBO Rep. 1, 477-478
63. Gozes, I., and Littauer, U. Z. (1978) Tubulin microheterogeneity increases with rat brain maturation. Nature 278, 411-413
64. Ginzburg, I., Behar, L., Givol, D., and Littauer, U. Z. (1981) The nucleotide sequence of rat α-tubulin: 3′-end characteristics, and evolutionary conservation. Nucleic Acids Res. 9, 2691-2697
65. Ginzburg, I., Scherson, T., Rybak, S., Kimhi, Y., Neuman, D., Schwartz, M., and Littauer, U. Z. (1983) Expression of mRNA for microtubule proteins in the developing nervous system. Cold Spring Harbor Symp. Quant. Biol. 48, 783-790
66. Teichman-Weinberg, A., Littauer, U. Z., and Ginzburg, I. (1988) The inhibition of neurite outgrowth in PC12 cells by tubulin antisense oligodeoyribonucleotides. Gene (Amst.) 72, 297-307
67. Littauer, U. Z., Giveon, D., Thierauf, M., Ginzburg, I., and Ponstingl, H. (1986) Common and distinct tubulin binding sites for microtubule-associated proteins. Proc. Natl. Acad. Sci. U. S. A. 83, 7162-7166
68. Kirsch, J., Zutra, A., and Littauer, U. Z. (1990) Characterization and intracellular distribution of microtubule-associated protein 2 in differentiating human neuroblastoma cells. J. Neurochem. 55, 1031-1041
69. Bushkin-Harav, I., Garty, N., and Littauer, U. Z. (1995) Down-regulation of a 67-kDa YIGSR-binding protein upon differentiation of human neuroblastoma cells. J. Biol. Chem. 270, 13422-13428
70. Kirsch, J., Langosch, D., Prior, P., Littauer, U. Z., Schmitt, B., and Betz, H. (1991) The 93-kDa glycine receptor-asociated protein binds to tubulin. J. Biol. Chem. 266, 22242-22245