The RNA binding properties of ‘native’ protein—protein complexes isolated from the <i>Escherichia coli</i> ribosome

Dijk, Jan; Littlechild, J.A.; Garrett, Roger A.

doi:10.1016/0014-5793(77)80255-x

Cited by 35 publications

(15 citation statements)

References 33 publications

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“…Earlier, we demonstrated that protein Lll and the complex L7/12-L10 independently associate with 23S RNA (9,10), and proposed that the capacity of the latter protein complex to bind specifically to the 23S RNA was an important criterion for its nativity (9). In the present work, we have localized the protein binding sites on a fragment of 23S RNA, demonstrated the interdependence of the RNA-binding of L7/12-L1O and Lii, and provided evidence that L10 constitutes a major RNA attachment site of the protein complex.…”

Section: Introductionmentioning

confidence: 99%

Studies on the binding of the ribosomal protein complex L7/12-L10 and protein L11 to the 5′-one third of 23S RNA: a functional centre of the 50S subunit

1979

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The RNA binding sites of the protein complex of L7/12 dimers and L10, and of protein L11, occur within the 5'-one third of 23S RNA. Binding of the L7/12-L10 protein complex to the 23S RNA is stimulated by protein L11 and vice-versa. This is the second example to be established of mutual stimulation of RNA binding by two ribosomal proteins or protein complexes, and suggests that this may be an important principle governing ribosomal protein-RNA assembly. When the L7/12-L10 complex is bound to the RNA, L10 becomes strongly resistant to trypsin. Since the L7/12 dimer does not bind specifically to the 23S RNA, this suggests that L10 constitutes a major RNA binding site of the protein complex. Only one of the L7/12 dimers is bound strongly in the (L7/12-L10)-23S RNA complex; the other can dissociate with no concurrent loss of L10.

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Section: Introductionmentioning

confidence: 99%

Studies on the binding of the ribosomal protein complex L7/12-L10 and protein L11 to the 5′-one third of 23S RNA: a functional centre of the 50S subunit

1979

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“…Evidence has also been presented that a dimer can be formed with S19 that binds 16S RNA at a specific site (9).…”

Section: Introductionmentioning

confidence: 99%

Evidence thatE. coliribosomal protein S13 has two separable functional domains involved in 16S RNA recognition and protein S19 binding

Schwarzbauer

Craven

1985

Nucl Acids Res

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We have found that E. coli ribosomal protein S13 recognizes multiple sites on 16S RNA.However, when protein S19 is included with a mixture of proteins S4, S7, S8, S16/S17 and S20, the S13 binds to the complex with measurably greater strength and with a stoichiometry of 1.5 copies per particle. This suggests that the protein may have two functional domains.We have tested this idea by cleaving the protein into two polypeptides. It was found that one of the fragments, composed of amino acid residues 84-117, retained the capacity to bind 16S RNA at multiple sites.Protein S19 had no affect on the strength or stoichiometry of the binding of this fragment. These data suggest that S13 has a C-terminal domain primarily responsible for RNA recognition and possibly that the N-terminal region is important for association with protein S19.

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“…when they are both present, a rather strong binding is observed (Dijk et al, 1977). RPS13 has two separable functional domains: whereas the N-terminal part is important for the association with RPS19 and forms a protein-binding domain for RPS19, the C-terminal part is primarily responsible for RNA recognition (Schwarzbauer and Craven, 1985).…”

Section: Discussionmentioning

confidence: 99%

“…In the Ecoli ribosome, RPS19 has been located on the head of the 30S subunit in close contact to ribosomal protein S 13 (reviewed by Wower et al, 1993). It has been shown that a heterodimer of RPS 19 and RPS 13 can be formed that binds tightly and specifically to 16S rRNA (Dijk et al, 1977). The N-terminal region of the S13 protein is important for the interaction with S 19 while the C-terminal part is involved in RNA binding (Schwarzbauer and Craven, 1985).…”

Section: Nuclear-encoded Rps13 Is Imported Into Chloroplastsmentioning

confidence: 99%

Transfer of rps19 to the nucleus involves the gain of an RNP-binding motif which may functionally replace RPS13 in Arabidopsis mitochondria.

et al. 1996

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The discovery of disrupted rps19 genes in Arabidopsis mitochondria prompted speculation about the transfer to the nuclear compartment. We here describe the functional gene transfer of rps19 into the nucleus of Arabidopsis. Molecular cloning and sequence analysis of rps19 show that the nuclear gene encodes a long N‐terminal extension. Import studies of the precursor protein indicate that only a small part of this extension is cleaved off during import. The larger part of the extension, which shows high similarity to conserved RNA‐binding domains of the RNP‐CS type, became part of the S19 protein. In the Escherichia coli ribosome S19 forms an RNA‐binding complex as heterodimer with S13. By using immuno‐analysis and import studies we show that a eubacterial‐like S13 protein is absent from Arabidopsis mitochondria, and is not substituted by either a chloroplastic or a cytosolic homologue of this ribosomal protein. We therefore propose that either a highly diverged or missing RPS13 has been functionally replaced by an RNP domain that most likely derived from a glycine‐rich RNA‐binding protein. These results represent the first case of a functional replacement of a ribosomal protein by a common RNA‐binding domain and offer a new view on the flexibility of biological systems in using well‐adapted functional domains for different jobs.

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The RNA binding properties of ‘native’ protein—protein complexes isolated from the Escherichia coli ribosome

Cited by 35 publications

References 33 publications

Studies on the binding of the ribosomal protein complex L7/12-L10 and protein L11 to the 5′-one third of 23S RNA: a functional centre of the 50S subunit

Studies on the binding of the ribosomal protein complex L7/12-L10 and protein L11 to the 5′-one third of 23S RNA: a functional centre of the 50S subunit

Evidence thatE. coliribosomal protein S13 has two separable functional domains involved in 16S RNA recognition and protein S19 binding

Transfer of rps19 to the nucleus involves the gain of an RNP-binding motif which may functionally replace RPS13 in Arabidopsis mitochondria.

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