Nucleic Acids Research, 1993, Vol. 21, No. 12 2891-2897
© 1993
MOLECULAR BIOLOGY |
Termination of translation in bacteria may be modulated via specific interaction between peptide chain release factor 2 and the last peptidyl-tRNASer/Phe
1Engelhardt Institute of Molecular Biology Moscow, Russia 2Institut Jacques Monod Paris, France
*To whom correspondence should be addressed at: Institut Jacques Monod, Universite Paris 7, Tour 43, 2 place Jussieu, 75251 Paris Cedex 05, France
Received February 25, 1993. Revised May 21, 1993. Accepted May 21, 1993.
The 5' context of 671 Escherichia coil stop codons UGA and UAA has been compared with the context of stop-like codons (UAC, UAU and CAA for UAA; UGG, UGC, UGU and CGA for UGA). We have observed highly significant deviations from the expected nucleotide distribution: adenine is over-represented whereas pyrimidines are under-represented in position –2 upstream from UAA. Uridine is over-represented in position –3 upstream from UGA. Lysine codons are preferable Immediately prior to UAA. A complete set of codons for serine and the phenylalanine UUC codon are preferable Immediately 5' to UGA. This non-random codon distribution before stop codons could be considered as a molecular device for modulation of translation termination. We have found that certain fragment of E.coll release factor 2 (RF2) (amino acids 93–114) is similar to the amino acid sequences of seryl-tRNA synthetase (positions 10–19 and 80–93) and of ß (small) subunit (positions 72–94) of phenylalanyl-tRNA synthetase from E. coll. Three-dimensional structure of E.coll seryl-tRNA synthetase is known [1]: its N-terminus represents an antiparallel 
-helical coiled-coil domain and contains a region homologous to RF2. On the basis of the above-mentioned results we assume that a specific Interaction between RF2 and the last peptidyl-tRNASer/Phe occurs during polypeptide chain termination in prokaryotic rlbosomes.
CiteULike 
Connotea 
Del.icio.us What's this?
This article has been cited by other articles:
|
|
 |
|
  A. G. Cridge, L. L. Major, A. A. Mahagaonkar, E. S. Poole, L. A. Isaksson, and W. P. Tate Comparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organisms Nucleic Acids Res., April 13, 2006; 34(7): 1959 - 1973. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. R. Cruz-Vera, E. Hernandez-Ramon, B. Perez-Zamorano, and G. Guarneros The Rate of Peptidyl-tRNA Dissociation from the Ribosome during Minigene Expression Depends on the Nature of the Last Decoding Interaction J. Biol. Chem., July 3, 2003; 278(28): 26065 - 26070. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. S. Hayes, B. Bose, and R. T. Sauer Proline Residues at the C Terminus of Nascent Chains Induce SsrA Tagging during Translation Termination J. Biol. Chem., September 6, 2002; 277(37): 33825 - 33832. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. N. Berezovsky, G. T. Kilosanidze, V. G. Tumanyan, and L. L. Kisselev Amino acid composition of protein termini are biased in different manners Protein Eng. Des. Sel., January 1, 1999; 12(1): 23 - 30. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. E. G. McCarthy Posttranscriptional Control of Gene Expression in Yeast Microbiol. Mol. Biol. Rev., December 1, 1998; 62(4): 1492 - 1553. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 B. C. Persson and J. F. Atkins Does Disparate Occurrence of Autoregulatory Programmed Frameshifting in Decoding the Release Factor 2 Gene Reflect an Ancient Origin with Loss in Independent Lineages? J. Bacteriol., July 1, 1998; 180(13): 3462 - 3466. [Abstract] [Full Text]
|
|
|
|
|
|
G. Grentzmann and P. J. Kelly Ribosomal Binding Site of Release Factors RF1 and RF2. A NEW TRANSLATIONAL TERMINATION ASSAY IN VITRO J. Biol. Chem., May 9, 1997; 272(19): 12300 - 12304. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. D. Roche and R. T. Sauer Identification of Endogenous SsrA-tagged Proteins Reveals Tagging at Positions Corresponding to Stop Codons J. Biol. Chem., July 20, 2001; 276(30): 28509 - 28515. [Abstract] [Full Text] [PDF]
|
|