Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1994 Jun 11;22(11):2166–2167. doi: 10.1093/nar/22.11.2166

A novel RNA-binding motif in omnipotent suppressors of translation termination, ribosomal proteins and a ribosome modification enzyme?

E V Koonin 1, P Bork 1, C Sander 1
PMCID: PMC308137  PMID: 7518079

Abstract

Using computer methods for database search, multiple alignment, protein sequence motif analysis and secondary structure prediction, a putative new RNA-binding motif was identified. The novel motif is conserved in yeast omnipotent translation termination suppressor SUP1, the related DOM34 protein and its pseudogene homologue; three groups of eukaryotic and archaeal ribosomal proteins, namely L30e, L7Ae/S6e and S12e; an uncharacterized Bacillus subtilis protein related to the L7A/S6e group; and Escherichia coli ribosomal protein modification enzyme RimK. We hypothesize that a new type of RNA-binding domain may be utilized to deliver additional activities to the ribosome.

Full text

PDF
2166

Selected References

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

  1. All-Robyn J. A., Brown N., Otaka E., Liebman S. W. Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein. Mol Cell Biol. 1990 Dec;10(12):6544–6553. doi: 10.1128/mcb.10.12.6544. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  3. Bairoch A. The PROSITE dictionary of sites and patterns in proteins, its current status. Nucleic Acids Res. 1993 Jul 1;21(13):3097–3103. doi: 10.1093/nar/21.13.3097. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Breining P., Piepersberg W. Yeast omnipotent supressor SUP1 (SUP45): nucleotide sequence of the wildtype and a mutant gene. Nucleic Acids Res. 1986 Jul 11;14(13):5187–5197. doi: 10.1093/nar/14.13.5187. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Didichenko S. A., Ter-Avanesyan M. D., Smirnov V. N. Ribosome-bound EF-1 alpha-like protein of yeast Saccharomyces cerevisiae. Eur J Biochem. 1991 Jun 15;198(3):705–711. doi: 10.1111/j.1432-1033.1991.tb16070.x. [DOI] [PubMed] [Google Scholar]
  6. Eustice D. C., Wakem L. P., Wilhelm J. M., Sherman F. Altered 40 S ribosomal subunits in omnipotent suppressors of yeast. J Mol Biol. 1986 Mar 20;188(2):207–214. doi: 10.1016/0022-2836(86)90305-0. [DOI] [PubMed] [Google Scholar]
  7. Gorbalenya A. E., Blinov V. M., Donchenko A. P., Koonin E. V. An NTP-binding motif is the most conserved sequence in a highly diverged monophyletic group of proteins involved in positive strand RNA viral replication. J Mol Evol. 1989 Mar;28(3):256–268. doi: 10.1007/BF02102483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Grenett H. E., Bounelis P., Fuller G. M. Identification of a human cDNA with high homology to yeast omnipotent suppressor 45. Gene. 1992 Jan 15;110(2):239–243. doi: 10.1016/0378-1119(92)90655-9. [DOI] [PubMed] [Google Scholar]
  9. Kang W. K., Icho T., Isono S., Kitakawa M., Isono K. Characterization of the gene rimK responsible for the addition of glutamic acid residues to the C-terminus of ribosomal protein S6 in Escherichia coli K12. Mol Gen Genet. 1989 Jun;217(2-3):281–288. doi: 10.1007/BF02464894. [DOI] [PubMed] [Google Scholar]
  10. Kolodrubetz D., Burgum A. Sequence and genetic analysis of NHP2: a moderately abundant high mobility group-like nuclear protein with an essential function in Saccharomyces cerevisiae. Yeast. 1991 Feb;7(2):79–90. doi: 10.1002/yea.320070202. [DOI] [PubMed] [Google Scholar]
  11. Koonin E. V., Bork P., Sander C. Yeast chromosome III: new gene functions. EMBO J. 1994 Feb 1;13(3):493–503. doi: 10.1002/j.1460-2075.1994.tb06287.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lalo D., Stettler S., Mariotte S., Slonimski P. P., Thuriaux P. Two yeast chromosomes are related by a fossil duplication of their centromeric regions. C R Acad Sci III. 1993;316(4):367–373. [PubMed] [Google Scholar]
  13. Leijonmarck M., Appelt K., Badger J., Liljas A., Wilson K. S., White S. W. Structural comparison of the prokaryotic ribosomal proteins L7/L12 and L30. Proteins. 1988;3(4):243–251. doi: 10.1002/prot.340030405. [DOI] [PubMed] [Google Scholar]
  14. Leijonmarck M., Liljas A. Structure of the C-terminal domain of the ribosomal protein L7/L12 from Escherichia coli at 1.7 A. J Mol Biol. 1987 Jun 5;195(3):555–579. doi: 10.1016/0022-2836(87)90183-5. [DOI] [PubMed] [Google Scholar]
  15. Rost B., Sander C. Prediction of protein secondary structure at better than 70% accuracy. J Mol Biol. 1993 Jul 20;232(2):584–599. doi: 10.1006/jmbi.1993.1413. [DOI] [PubMed] [Google Scholar]
  16. Schuler G. D., Altschul S. F., Lipman D. J. A workbench for multiple alignment construction and analysis. Proteins. 1991;9(3):180–190. doi: 10.1002/prot.340090304. [DOI] [PubMed] [Google Scholar]
  17. Stansfield I., Grant G. M., Akhmaloka, Tuite M. F. Ribosomal association of the yeast SAL4 (SUP45) gene product: implications for its role in translation fidelity and termination. Mol Microbiol. 1992 Dec;6(23):3469–3478. doi: 10.1111/j.1365-2958.1992.tb01782.x. [DOI] [PubMed] [Google Scholar]
  18. Tassan J. P., Le Guellec K., Kress M., Faure M., Camonis J., Jacquet M., Philippe M. In Xenopus laevis, the product of a developmentally regulated mRNA is structurally and functionally homologous to a Saccharomyces cerevisiae protein involved in translation fidelity. Mol Cell Biol. 1993 May;13(5):2815–2821. doi: 10.1128/mcb.13.5.2815. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Vincent A., Liebman S. W. The yeast omnipotent suppressor SUP46 encodes a ribosomal protein which is a functional and structural homolog of the Escherichia coli S4 ram protein. Genetics. 1992 Oct;132(2):375–386. doi: 10.1093/genetics/132.2.375. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wilson K. S., Appelt K., Badger J., Tanaka I., White S. W. Crystal structure of a prokaryotic ribosomal protein. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7251–7255. doi: 10.1073/pnas.83.19.7251. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES