Fragment of protein L18 from the Escherichia coli ribosome that contains the 5S RNA binding site

Newberry, Veronica; Brosius, Jürgen; Garrett, Roger A.

doi:10.1093/nar/5.6.1753

Cited by 22 publications

(11 citation statements)

References 26 publications

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“…16117 to 117 of EL18 retains the capability to bind to the 5 S rRNA, and it was therefore concluded that the N-terminal region, pos. 1-16, is not essential for the L18-5 S rRNA interaction [13]. Our result on the comparison of the amino acid sequences of EL18 and BL18 is quite consistent with this conclusion, showing that the C-terminal two-third is well conserved in contrast to the N-terminal region.…”

Section: Comparison Of Amino Acid Sequencessupporting

confidence: 88%

“…For instance, the complete amino acid sequences of the three proteins (EL5, EL18, and EL25), which specifically bind to the 5 S rRNA, have been determined [lo-121. Furthermore, a fragment of protein EL18 that retains the capability to bind to the 5 S rRNA was prepared by limited tryptic digestion and sequenced [13]. In addition to the 5 S rRNA binding proteins from E. coli [14].…”

Section: Stearothermophilusmentioning

confidence: 99%

“…This may be a reflection of the functional or structural significance of these residues. Newberry et al [13] have proposed that the N-terminal region of L18 might be involved in either the interaction with the other 5 S rRNA binding proteins L5 and L25, or the attachment of the 5 S rRNA-protein complex to the 23 S rRNA.…”

Section: Comparison Of Amino Acid Sequencesmentioning

confidence: 99%

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The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 from the moderate thermophile Bacillus stearothermophilus ribosome

Kimura

1987

FEBS Letters

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The complete amino acid sequences of the 5 S rRNA binding proteins LS and L18 isolated from ribosomes of the moderate thermophile Bacillus stearothermophilus are presented. This has been achieved by the sequence analysis of peptides derived by enzymatic digestions with trypsin, chymotrypsin, pepsin, and Staphylococcus aureus protease, as well as by chemical cleavage with cyanogen bromide. The proteins LS and L18 consist of 179 and 120 amino acid residues, and have M, values of 20 163 and 13 473, respectively. A comparison of the sequences with their counterparts from the Escherichia cofi ribosome reveals 59% identical residues for LS, and 53% for L 18. For both proteins, the distribution of conserved regions is not random along the protein chains: some regions are highly conserved while others are not. The regions which are conserved during evolution may be important for the interaction with the 5 S rRNA molecule.5 S rRNA binding protein; Amino acid sequence; Primary structure; (Bacillus stearothermophilus)

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Section: Comparison Of Amino Acid Sequencessupporting

confidence: 88%

Section: Stearothermophilusmentioning

confidence: 99%

Section: Comparison Of Amino Acid Sequencesmentioning

confidence: 99%

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The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 from the moderate thermophile Bacillus stearothermophilus ribosome

Kimura

1987

FEBS Letters

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“…At present the mechanism of this interaction is not understood although it has been proposed either that the proteins form a link between the RNA's (2,5), or that intermolecular RNA-RNA interactions occur (6) possibly as a consequence of protein-induced conformational changes in the 5S RNA which are known to occur (7 -9).…”

Section: Introductionmentioning

confidence: 99%

“…L18 is essential for 5S RNA -23S RNA interaction (2, 4) and we have shown, in a trypsin digestion study of an L18 -5S RNA complex, that whereas the C-terminal part of L18 (residues 18 to 117) contains the primary 5S RNA binding site, the highly basic N-terminal region is accessible (5). We proposed, therefore, that this region of L18 may play a role, direct or indirect, in the interaction with 23S RNA.…”

Section: Introductionmentioning

confidence: 99%

The role of the basic N-terminal region of protein L18 in 5S RNA–23S RNA complex formation

Newberry

Garrett

1980

Nucl Acids Res

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Of the three proteins, L5, L18 and L25, which bind to 5S RNA, the former two effect the interaction of 5S RNA with 23S RNA. We have used trypsin as a probe to investigate the roles of the proteins in this RNA-RNA assembly, with the following results:(1) In complexes with 5S RNA, the highly basic N-terminal region of L18 is accessible to trypsin. This accessibility is unaffected by L25. However, its presence is essential for stimulating L5 binding. (2) In 5S RNA-protein-23S RNA complexes proteins L5 and L18 are both strongly resistant to proteolysis. (3) No 5S RNA-23S RNA complex formation occurs in the presence of L5 and the C-terminal L18 fragment. Two possible models for the mechanism of RNA-RNA assembly are proposed.

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Does unpaired adenosine-66 from helix II of Escherichia coli 5S RNA bind to protein L18?

Christiansen¹,

Douthwaite²,

Christensen³

et al. 1985

The EMBO Journal

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Adenosine-66 is unpaired within helix II of Escherichia coli 5S RNA and lies in the binding site of ribosomal protein L18. It has been proposed as a recognition site for protein L18. We have investigated further the structural importance of this nucleotide by deleting it. The 5S RNA gene of the rrnB operon of E. coli was subjected to primer-directed mutagenesis. To produce the deletion it was necessary to use simultaneously the mutagenic dodecamer dCGGCGCACGGCG and the universal M13 primer dCCCAGTCACGACGYI, and to employ forced annealing conditions. The mutated gene was expressed in an overproducing plasmid derived from pKK3535. Binding studies with protein L18 revealed that the protein bound much more weakly to the mutated 5S RNA. We consider the most likely explanation of this result is that L18 interacts with adenosine-66, and we present a tentative model for an interaction between the unpaired adenosine and the adjacent guanosine-67 of the RNA and glutamine-19 of the protein L18.

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Fragment of protein L18 from the Escherichia coli ribosome that contains the 5S RNA binding site

Cited by 22 publications

References 26 publications

The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 from the moderate thermophile Bacillus stearothermophilus ribosome

The complete amino acid sequences of the 5 S rRNA binding proteins L5 and L18 from the moderate thermophile Bacillus stearothermophilus ribosome

The role of the basic N-terminal region of protein L18 in 5S RNA–23S RNA complex formation

Does unpaired adenosine-66 from helix II of Escherichia coli 5S RNA bind to protein L18?

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