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PMID: 6340066 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Nuclease mapping of the secondary structure of the 49-nucleotide 3' terminal cloacin fragment of Escherichia coli 16s RNA and its interactions with initiation factor 3.

Nucleic acids research ·Vol. 11 ·No. 7 ·1983-04-11 ·Pages 2035-52

Wickstrom E

Abstract

Escherichia coli translational initiation factor 3 (IF3) may be crosslinked to the 3' end of 16S RNA in 30S ribosomal subunits. In order to determine the sequence to which IF3 may bind in vivo, samples of 5'-32P labelled 3' terminal 49-nucleotide fragment of 16S RNA were incubated 5 min. at 37 degrees in 40 mM Tris-HOAc, pH 7.4, 100 mM NaCl, 1 mM Mg (OAc)2, 1 mM ZnSO4, with or without IF3, then reacted a further 5 min with nuclease S1, RNase T1, or RNase A. Base pairing between the 5' and 3' legs of the fragment occurs in the absence of IF3, but is disrupted by IF3 binding. IF3 appears to protect some residues near the 5' end of the fragment (U1495, A1499, A1500, A1502, and A1503) from nuclease S1, and potentiates S1 attack on others (G1494, G1497, C1501, G1504, G1505, U1506, G1517, G1529, G1530, and C1533). A series of equimolar reactions at increasing dilution imply an association constant range of 1.4-7.0 X 10(7) M-1.

MeSH Terms
Bacteriocins/genetics Base Sequence Cloacin/genetics Escherichia coli/genetics Nucleic Acid Conformation Peptide Initiation Factors/genetics Prokaryotic Initiation Factor-3 RNA, Ribosomal/genetics Ribosomal Proteins/genetics
Chemicals
Bacteriocins Peptide Initiation Factors Prokaryotic Initiation Factor-3 RNA, Ribosomal Ribosomal Proteins Cloacin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Wickstrom E
References (44)
44 references, click to expand
  1. Escherichia coli initiation factor IF3 binding to AUG and AUG-containing single strands and hairpin loops, and nonspecific binding to polymers.
    Biochim Biophys Acta. 1974 Apr 27;349(1):125-30 PMID: 11400430
  2. Initiation of protein synthesis in Escherichia coli. I. Purification and properties of the initiation factors.
    Cold Spring Harb Symp Quant Biol. 1969;34:285-90 PMID: 4909505
  3. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites.
    Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342-6 PMID: 4598299
  4. The stability of RNA hairpin loops containing A-U-G: An-U-G-Um.
    Biopolymers. 1974 Nov;13(11):2367-83 PMID: 4429788
  5. Binding of ribosomal protein S1 of Escherichia coli to the 3' end of 16S rRNA.
    Proc Natl Acad Sci U S A. 1975 Aug;72(8):2940-4 PMID: 1103129
  6. New aspects of the IF3-ribosome interaction.
    FEBS Lett. 1976 Feb 15;62(2):111-4 PMID: 767141
  7. 30S ribosomal proteins associated with the 3'-terminus of 16S RNA.
    FEBS Lett. 1975 Oct 15;58(1):281-4 PMID: 1225593
  8. The specific role of ribosomal protein S1 in the recognition of native phage RNA.
    Eur J Biochem. 1976 May 1;64(2):511-8 PMID: 776620
  9. Near neighbors of IF3 bound to 30S ribosomal subunits.
    FEBS Lett. 1975 Nov 15;59(2):287-90 PMID: 776666
  10. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding.
    Anal Biochem. 1976 May 7;72:248-54 PMID: 942051
  11. Cross-linking of initiation factor IF3 to proteins of the Escherichia coli 30 S ribosomal subunit.
    J Mol Biol. 1976 Aug 5;105(2):219-30 PMID: 823340
  12. The 3'-terminus of 16 S ribosomal RNA of Escherichia coli. Isolation and purification of the terminal 49-nucleotide fragment at a milligram scale.
    FEBS Lett. 1976 Dec 1;71(2):351-5 PMID: 793864
  13. Purification and characterization of a complex between cloacin and its immunity protein isolated from Enterobacter cloacae (Clo DF13). Dissociation and reconstitution of the complex.
    Eur J Biochem. 1977 Feb 15;73(1):107-14 PMID: 402267
  14. Protection of specific sites in 16 S RNA from chemical modification by association of 30 S and 50 S ribosomes.
    J Mol Biol. 1977 Jan 5;109(1):131-49 PMID: 839533
  15. High-resolution proton magnetic resonance study of the secondary structure of the 3'-terminal 49-nucleotide fragment of 16S rRNA from Escherichia coli.
    Proc Natl Acad Sci U S A. 1977 Mar;74(3):1028-31 PMID: 322143
  16. Ribosome structure: localization of N6,N6-dimethyladenosine by electron microscopy of a ribosome-antibody complex.
    Proc Natl Acad Sci U S A. 1977 Apr;74(4):1468-72 PMID: 323854
  17. Requirement of chain initiation factor 3 and ribosomal protein S1 in translation of synthetic and natural messenger RNA.
    Nucleic Acids Res. 1977 Jan;4(1):17-29 PMID: 325517
  18. Specific binding site of e. coli initiation factor 3 (IF3) at a 3'-terminal region of MS2 RNA.
    Nature. 1977 Jun 9;267(5611):550-2 PMID: 327333
  19. The primary structure of the initiation factor IF-3 from Escherichia coli.
    FEBS Lett. 1977 Jul 15;79(2):269-75 PMID: 330233
  20. Purification and characterization of protein synthesis initiation factors IF1, IF2, and IF3 from Escherichia coli.
    Arch Biochem Biophys. 1977 Aug;182(2):626-38 PMID: 332085
  21. Escherichia coli ribosomal protein S1 has two polynucleotide binding sites.
    Proc Natl Acad Sci U S A. 1977 Nov;74(11):4786-90 PMID: 337301
  22. On the relationship between the binding of ribosomal protein S1 to the 30 S subunit of Escherichia coli and 3' terminus of 16 S RNA.
    J Mol Biol. 1978 Jun 5;121(4):411-30 PMID: 353289
  23. The relationship between the 3'-end of 16 S RNA and the binding of initiation factor IF-3 to the 30 S subunit of E. coli.
    FEBS Lett. 1978 Jul 15;91(2):265-8 PMID: 354964
  24. Complete nucleotide sequence of a 16S ribosomal RNA gene from Escherichia coli.
    Proc Natl Acad Sci U S A. 1978 Oct;75(10):4801-5 PMID: 368799
  25. Interaction of Escherichia coli ribosomal protein S1 with ribosomes.
    Proc Natl Acad Sci U S A. 1979 Mar;76(3):1040-4 PMID: 375222
  26. The 3' terminus of 16S rRNA: secondary structure and interaction with ribosomal protein S1.
    Nucleic Acids Res. 1979 Dec 20;7(8):2399-418 PMID: 392471
  27. Stoichiometry of homopolynucleotide binding to Escherichia coli translational initiation factor 3.
    Arch Biochem Biophys. 1980 Mar;200(1):296-300 PMID: 6987955
  28. Circular dichroism study of Escherichia coli initiation factor 3 binding to nucleic acids.
    Biochemistry. 1980 Sep 16;19(19):4486-92 PMID: 6996719
  29. Studies on the function of two adjacent N6,N6-dimethyladenosines near the 3' end of 16 S ribosomal RNA of Escherichia coli. II. The effect of the absence of the methyl groups on initiation of protein biosynthesis.
    J Biol Chem. 1979 Sep 25;254(18):9090-3 PMID: 383711
  30. Ribosome structure: localization of 3' end of RNA in small subunit by immunoelectronmicroscopy.
    Proc Natl Acad Sci U S A. 1979 Aug;76(8):3769-73 PMID: 386348
  31. Secondary structure model for bacterial 16S ribosomal RNA: phylogenetic, enzymatic and chemical evidence.
    Nucleic Acids Res. 1980 May 24;8(10):2275-93 PMID: 6159576
  32. Optimal computer folding of large RNA sequences using thermodynamics and auxiliary information.
    Nucleic Acids Res. 1981 Jan 10;9(1):133-48 PMID: 6163133
  33. The conformation of chicken, rat and human U1A RNAs in solution.
    Nucleic Acids Res. 1981 Feb 25;9(4):841-58 PMID: 6164982
  34. IF-3 crosslinking to Escherichia coli ribosomal 30 S subunits by three different light-dependent procedures: identification of 30 S proteins crosslinked to IF-3--utilization of a new two-stage crosslinking reagent, p-nitrobenzylmaleimide.
    Arch Biochem Biophys. 1981 May;208(2):554-62 PMID: 7020604
  35. Physical parameters of Escherichia coli translational initiation factor 3 binding to poly(A).
    FEBS Lett. 1981 Jun 1;128(1):154-6 PMID: 7023978
  36. Secondary structure comparisons between small subunit ribosomal RNA molecules from six different species.
    Nucleic Acids Res. 1981 Aug 11;9(15):3621-40 PMID: 7024918
  37. Fluorescence polarization studies of the interaction of Escherichia coli protein synthesis initiation factor 3 with 30S ribosomal subunits.
    Biochemistry. 1981 Sep 29;20(20):5859-65 PMID: 7028112
  38. Destabilization of secondary structure in 16S ribosomal RNA by dimethylation of two adjacent adenosines.
    Nucleic Acids Res. 1981 Sep 11;9(17):4413-22 PMID: 7029465
  39. The topographical localization of IF3 on Escherichia coli 30 S ribosomal subunits as a clue to its way of functioning.
    FEBS Lett. 1982 Jan 25;137(2):163-7 PMID: 7037454
  40. Sequence, modified nucleotides and secondary structure at the 3'-end of small ribosomal subunit RNA.
    Nucleic Acids Res. 1982 Feb 25;10(4):1149-58 PMID: 6175952
  41. Expression of the gene for Escherichia coli initiation factor IE-3 in vivo and in vitro.
    Eur J Biochem. 1982 Apr;123(3):483-8 PMID: 7042344
  42. A carbon-13 nuclear magnetic resonance study of the 3'-terminus of 16S ribosomal RNA of Escherichia coli specifically labeled with carbon-13 in the methylgroups of the m6(2)Am6(2)A sequence.
    Nucleic Acids Res. 1982 Jul 24;10(14):4237-45 PMID: 6750555
  43. Sequence of a 1.26-kb DNA fragment containing the structural gene for E.coli initiation factor IF3: presence of an AUU initiator codon.
    EMBO J. 1982;1(3):311-5 PMID: 6325158
  44. Localization of the decoding region on the 30S Escherichia coli ribosomal subunit by affinity immunoelectron microscopy.
    Proc Natl Acad Sci U S A. 1979 Mar;76(3):1054-8 PMID: 375223
Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
Published
1983-04-11
Pages
2035-52
Language
English
Region
England
NLM ID
0411011
PMCID
PMC325860
Subset
IM
Grants
NIGMS NIH HHS · GM-24128 · United States
NIGMS NIH HHS · GM-28408 · United States
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