Amino acid replacements in proteins S5 and S12 of two Escherichia coli revertants from streptomycin dependence to independence

Itoh, Takuzì; Wittmann, H. G.

doi:10.1007/bf00267779

Cited by 54 publications

(27 citation statements)

References 21 publications

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“…The order of T2-T 16 was known from mutants of S5 in which Argr 1 1 is replaced by leucine in the mutant N-421 [35] and in d-1023 [36]. The same result came from analysis of mutant nea3 19 where this arginine residue is replaced by serine and from nea3 14 where it is exchanged by glycine [37].…”

Section: Alignment Of the Isolated Peptidesmentioning

confidence: 97%

“…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%

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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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Section: Alignment Of the Isolated Peptidesmentioning

confidence: 97%

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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“…In an earlier study, we identified a unique mutation in r-protein S5 [at a universally conserved position (28 in Escherichia coli) where glycine is mutated to aspartate] (8) that is distinct from other identified S5 ram mutations (9,10). The mutation, G28D, not only decreases translational fidelity but also results in cold sensitivity and accumulation of precursor SSUs, both characteristics of defects in the SSU biogenesis cascade (8).…”

mentioning

confidence: 99%

Appropriate maturation and folding of 16S rRNA during 30S subunit biogenesis are critical for translational fidelity

Roy-Chaudhuri

Kirthi

Culver

2010

Proc. Natl. Acad. Sci. U.S.A.

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Ribosomal protein S5 is critical for small ribosomal subunit (SSU) assembly and is indispensable for SSU function. Previously, we identified a point mutation in S5, (G28D) that alters both SSU formation and translational fidelity in vivo, which is unprecedented for other characterized S5 mutations. Surprisingly, additional copies of an extraribosomal assembly factor, RimJ, rescued all the phenotypes associated with S5(G28D), including fidelity defects, suggesting that the effect of RimJ on rescuing the miscoding of S5(G28D) is indirect. To understand the underlying mechanism, we focused on the biogenesis cascade and observed defects in processing of precursor 16S (p16S) rRNA in the S5(G28D) strain, which were rescued by RimJ. Analyses of p16S rRNA-containing ribosomes from other strains further supported a correspondence between the extent of 5 0 end maturation of 16S rRNA and translational miscoding. Chemical probing of mutant ribosomes with additional leader sequences at the 5 0 end of 16S rRNA compared to WT ribosomes revealed structural differences in the region of helix 1. Thus, the presence of additional nucleotides at the 5 0 end of 16S rRNA could alter fidelity by changing the architecture of 16S rRNA in translating ribosomes and suggests that fidelity is governed by accuracy and completeness of the SSU biogenesis cascade.R-protein S5 | ram mutations | ribosome biogenesis | 16S rRNA processing O ne of the most remarkable feats of the ribosome is the ability to decode genetic information accurately in a process that involves the interaction of aminoacyl-transfer RNAs (aa-tRNAs) to the aa-tRNA binding site (A site) on the small ribosomal subunit (SSU; 30S). However, this process is not fully error proof and missense errors occur at a frequency of 10 −3 to 10 −4 per amino acid synthesized (1). Decoding is thought to involve a number of local and global conformational changes in the SSU upon binding of a cognate aa-tRNA to the A site. These structural changes result in a transition from the "open" to the "closed" form whereby the head of the SSU rotates toward the shoulder and the shoulder toward the platform (2). The r-proteins S4, S5, and S12 along with helices 27 and 44 of 16S rRNA are implicated in fidelity; mutations in S4 and S5 can lead to ribosome ambiguity (ram) or miscoding, whereas specific mutations in S12 lead to hyperaccuracy (3). Based on the recent crystal structures (2), the r-protein ram mutations map at the interface of S4 and S5 and disrupt a number of salt bridges that are present in the open SSUs. These changes could destabilize the open state, thereby perturbing the equilibrium to promote the closed state and allowing decreased discrimination in the decoding process (4). Some additional biochemical and structural data support this model (5); nonetheless, other data are hard to incorporate into this scheme. A few mutations in S4 can confer "restrictive" phenotypes to Salmonella typhimurium (6) and surprisingly these hyperaccurate alleles of S4 suppress the hyperaccurate phenotypes of S1...

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“…Amino acid sequence analyses have been done for many altered Sl 2 proteins isolated from streptomycin resistant mutants [8,9], from streptomycin dependent mutants [10,11] and from neamine resistant mutants [13]. The results from these studies show that the amino acid replacements are restricted to only two regions of SI 2: Lys at position 42 and a short region from position 85-91.…”

Section: Resultsmentioning

confidence: 99%

“…The tryptic peptides of protein S12 have been isolated and their amino acid compositions reported [8,10]. The amino acid sequence of the N-terminal region of S12 has been determined [ 14,151.…”

Section: Introductionmentioning

confidence: 99%

Primary structure of protein S12 from the smallEscherichia coli ribosomal subunit

1977

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Amino acid replacements in proteins S5 and S12 of two Escherichia coli revertants from streptomycin dependence to independence

Cited by 54 publications

References 21 publications

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

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

Appropriate maturation and folding of 16S rRNA during 30S subunit biogenesis are critical for translational fidelity

Primary structure of protein S12 from the smallEscherichia coli ribosomal subunit

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