Ribosomal proteins

Funatsu, Gunki; Puls, W; Schiltz, Emil; Reinbolt, Joseph; Hg, Wittmann

doi:10.1007/bf00277293

Cited by 54 publications

(11 citation statements)

References 14 publications

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“…However, several proteins were missing from the assembled 30 S subunit, possibly because the RI intermediate failed to undergo the RI 3 RI* activation step necessary for complete assembly (34). Deletions of the C terminus have been selected in several laboratories as pseudorevertants from S12 mutants that are streptomycin-dependent (35)(36)(37). The mutant proteins generally are shorter than wild type by 20 -30 amino acids, bind 16 S rRNA less strongly than wild type S4 (38,39), and tend to be temperature sensitive for ribosome assembly (10).…”

Section: Comparison Of 16 S Rrna and ␣ Mrna Binding By S4mentioning

confidence: 99%

Messenger RNA Recognition by Fragments of Ribosomal Protein S4

Baker

Draper

1995

Journal of Biological Chemistry

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Ribosomal protein S4 from Escherichia coli binds a large domain of 16 S ribosomal RNA and also a pseudoknot structure in the ␣ operon mRNA, where it represses its own synthesis. No similarity between the two RNA binding sites has been detected. To find out whether separate protein regions are responsible for rRNA and mRNA recognition, proteins with N-terminal or C-terminal deletions have been overexpressed and purified. Protein-mRNA interactions were detected by (i) a nitrocellulose filter binding assay, (ii) inhibition of primer extension by reverse transcriptase, and (iii) a gel shift assay. Circular dichroism spectra were taken to determine whether the proteins adopted stable secondary structures. From these studies it is concluded that amino acids 48 -104 make specific contacts with the mRNA, although residues 105-177 (out of 205) are required to observe the same toeprint pattern as fulllength protein and may stabilize a specific portion of the mRNA structure. These results parallel ribosomal RNA binding properties of similar fragments (Conrad, R. C., and Craven, G. R. (1987) Nucleic Acids Res. 15, 10331-10343, and references therein). It appears that the same protein domain is responsible for both mRNA and rRNA binding activities.Functional studies of ribosomes have tended to focus on the roles of the ribosomal RNAs in recent years, as a number of studies have uncovered specific contributions of different rRNA domains to ribosome activities (1). As more ribosomal protein sequences have become available, it is becoming clear that a number of these proteins are highly conserved among all organisms and must also have specific and necessary roles in ribosome function. An intriguing set of ribosomal proteins are those that bind directly and independently to the ribosomal RNAs and also autogeneously regulate ribosomal protein expression. In many cases the regulation is due to the protein recognition of the mRNA translational initiation region (2), although protein binding to a pre-mRNA splice site has also been observed (3). These instances of a single protein carrying out two different RNA-related functions provide interesting systems for studying how RNA recognition has evolved and is related to specific protein functions (4).In several instances there is convincing similarity between the secondary structures of the mRNA and rRNA targets of an autoregulatory ribosomal protein (4 -6). It is reasonable to conclude that both mRNA and rRNA bind in the same active site of any one of these proteins. In other cases there is no obvious similarity between the two RNA substrates. For instance, the mRNA target site for Escherichia coli S4 protein is a complex pseudoknot of about 110 nucleotides within the ␣ operon mRNA (7). Nearly the entire 5Ј domain of the 16 S rRNA, a fragment of 460 nucleotides, is needed to form the ribosomal binding site for the protein (8), although a smaller region is protected from cleavage by bound protein (9). There is no primary or secondary structural similarity between the two target sites, ...

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Section: Comparison Of 16 S Rrna and ␣ Mrna Binding By S4mentioning

confidence: 99%

Messenger RNA Recognition by Fragments of Ribosomal Protein S4

Baker

Draper

1995

Journal of Biological Chemistry

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“…The results are summarized in fig.4. Similar to mutants altered in protein S12 [40], the amino acid exchanges in mutationally altered S5 proteins are clustered in a few regions of the protein chain; in positions 19-21 for four spectinomycin-resistant mutants [34,41,42]: in positions 103 and 111 for three revertants from streptomycin-dependence to independence [35,36] and in position 111 for two neamycin-resistant mutants [37]. Protein S5 of mutant sup O-1 in which the temperature-sensitive phenotype of an alanyltRNA synthetase mutation is partially suppressed, is shortened by five amino acids at the C-terminus and terminates with -Ser-Val-Gly [35].…”

Section: Comparison Of Protein S5 With Other Ribosomal Proteinsmentioning

confidence: 99%

The primary structure of protein S5 from the small subunit of the Escherichia coli ribosome

Wittmann‐Liebold

Greuer

1978

FEBS Letters

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“…It should also be interesting to perform similar experiments with ribosomal proteins from heatresistant bacteria like Bacillus thermophilus and also with proteins from any mutants which contain modified ribosomal proteins [46,47], particularly assemblydefective mutant S4 [48]. This should give clues to the relative importance of the protein conformational transition in ribosome assembly.…”

Section: Relation With the Reconstitution Of30-s Ribosomal Subunitmentioning

confidence: 99%

Effect of Reconstitution Conditions on the Structure of Escherichia coli 30‐S Ribosomal‐Subunit Components

Lemieux

Lefèvre

Daune

1974

European Journal of Biochemistry

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16-S RNA and five pure ribosomal proteins (S3, S4, S6, S7 and S8) from Escherichia coli 30-S subunits were studied by circular dichroism in regard to the reconstitution of biologically active subunits. A small structural variation upon heating could be measured for RNA. It cannot be interpreted in terms of stacking or disruption of hydrogen bonds. However, most proteins underwent important structural modifications when heated to 42 "C in reconstitution solvent. This effect was not dependent on the presence of magnesium salt. The relative amounts of secondary structure of native and heat-denatured ribosomal proteins were calculated by using three reference curves obtained from standard proteins, the exact secondary structure of which has been determined by X-ray crystallography. In contrast with earlier results, about 18 % p-structure was detected in native proteins.This discrepancy can most probably be attributed to the calculation method used. Results are discussed in relation to reconstitution of ribosomes.

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Ribosomal proteins

Cited by 54 publications

References 14 publications

Messenger RNA Recognition by Fragments of Ribosomal Protein S4

Messenger RNA Recognition by Fragments of Ribosomal Protein S4

The primary structure of protein S5 from the small subunit of the Escherichia coli ribosome

Effect of Reconstitution Conditions on the Structure of Escherichia coli 30‐S Ribosomal‐Subunit Components

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