Comparative immunological and electrophoretic studies on ribosomal proteins of Bacillaceae

Geisser, M.; Tischendorf, Gilbert; Stöffler, Georg

doi:10.1007/bf00333661

Cited by 72 publications

(15 citation statements)

References 16 publications

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“…As shown in Fig. 2B, the relC strain 61953 lacked BS-L11 (marked by arrow), a result reported previously (34), and the patterns of protein spots in the gel were similar to those reported earlier (8,38). Accordingly, the ribosomal proteins of the Streptomyces rel mutants were then compared with those of the wild type.…”

Section: Resultssupporting

confidence: 90%

Streptomyces relC mutants with an altered ribosomal protein ST-L11 and genetic analysis of a Streptomyces griseus relC mutant

Ochi

1990

J Bacteriol

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Several relaxed (rel) mutants have been obtained front Streptomyces species by selecting colonies resistant to thiopeptin, an analogue of thiostrepton. Using two-dimensional gel electrophoresis, I compared the ribosomal proteins from rel and rel pairs of S. antibioticus, S, lavendudae, S. gnseoflavus, and S. griseus. It was found that all of the Streptomyces rel mutants thus examined had an altered or missing ribosomal protein, designated tentatively ST-Lll. These rel mutants therefore could be classified as reiC mutants and were highly sensitive to erythromycin or high temperature. A reiC mutant of S. griseus was defective in streptomycin production, but phenotypic reversion of this defect to normal productivity was found at high incidence among progeny of the reiC mutant. This phenotypic reversion did not accompany a reappearance of ribosomal protein ST-Lll, and furthermore the ability of accumulating ppGpp still remained at a low level, thus suggesting existence of a mutation (named sup) which suppresses the streptomycin deficiency phenotype exhibited by the reiC mutant. Genetic analysis revealed that there i a correlation between the rel ntutation and the inability to produce streptomycin or aerial mycelia. The sup mutation was found to lie at a chromosomal locus distinct from that of the reiC mutation. It was therefore concluded that the dependence of streptomycin production on the normal function of the reiC gene could be entirely bypassed by a mutation at the suppressor locus (sup). The suppressing effect of the sup mutation on the reiC mutation was blocked when the afs mutation (defective in A-factor synthesis) was introduced into a reiC sup double mutant. It is proposed that the sup gene or its product can be a direct or indirect target for ppGpp.The study of differentiation in Streptomyces species is of interest because they produce numerous antibiotics (physiological differentiation), usually in the process of aerial mycelium formation (morphological differentiation). The couipling of morphological and physiological differentiation suggests a mechanistic connection, clarification of which has only been attempted (for reviews, see references 3 and 14). Especially, it is frequently observed and widely accepted that morphological and physiological differentiation start concomitantly in response to nutrient limitation. One of the significant bacterial regulatory systems, coupled to nutrient limitation, is "stringent response," which causes immediate cessation of RNA synthesis and of other cellular reactions (for reviews, see references 2, 7, and 32). The guanine nucleotides ppGpp (guanosine 5'-diphosphate-3'-diphosphate) and pppGpp (guanosine 5'-triphosphate-3'-diphosphate) are believed to be responsible for this stringent response (9) mechanism of stringent response, briefly noted above, is probably oversimplified. Recent investigations suggest that in E. coli a "relaxed response" is not simply the absence of a stringent response; instead, in a relA relaxed strain, ppGpp levels drop precipitously rather ...

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Section: Resultssupporting

confidence: 90%

Streptomyces relC mutants with an altered ribosomal protein ST-L11 and genetic analysis of a Streptomyces griseus relC mutant

Ochi

1990

J Bacteriol

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“…Some of the critical ribosomal proteins in B. subtilis have not been identified or genetically mapped. For example, Bacillus ribosomal protein BL9 is equivalent to the E. coli L7/L12 (Geisser et al 1973) but its genetic location has not been fixed; likewise, the Bacillus equivalent of protein L10 is unknown. On the other hand, BL11 has been shown to correspond to E. coli Ll 1 (Wiener et al 1979) and is placed similarly on the genetic map.…”

Section: Discussionmentioning

confidence: 97%

“…1973) and assuming 87% of the cellular RNA to be rRNA. The ratio of a r l a p was then taken as the ratio of r protein per cell to RNA polymerase protein per cell corrected for the molecular weight of all peptides in each assembly (Geisser et al 1973;Doi 1977). French press treatment of concentrated cell pellets such as those used for polymerase determination caused considerable loss of sample due to the small sample size.…”

Section: Additional Methodsmentioning

confidence: 99%

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Relationship between synthesis of ribosomes and RNA polymerase in Bacillus subtilis

Leduc¹,

Hoekstra²,

Spiegelman³

1982

Can. J. Microbiol.

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The relationship between RNA polymerase synthesis and ribosome synthesis has been investigated in Bacillus subtilis growing at different rates. The amount of polymerase was determined by quantitation of polymerase subunits on polyacrylamide gels, while ribosome synthesis was estimated from accumulation of total RNA. The ratio of ribosome to RNA polymerase synthesis was 5:1 at slower growth rates and increased with growth rate. Bacillus subtilis was estimated to contain between 10-and 2-fold excess of RNA polymerase depending on its growth rate.

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“…In this system, the acidic proteins ofB. subtilis migrate where indicated in the upper left corners of the plates and usually give a very faint spot in Bacillus ribosomes [5,17]. However, a good part of these proteins is retained on the I-D gel rod and, as fig.2 shows (arrows), in the spore ribosomes there are no acidic proteins present.…”

Section: Resultsmentioning

confidence: 99%

Alteration of the acidic ribosomal proteins from dormant spores of Bacillus subtilis

1976

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Comparative immunological and electrophoretic studies on ribosomal proteins of Bacillaceae

Cited by 72 publications

References 16 publications

Streptomyces relC mutants with an altered ribosomal protein ST-L11 and genetic analysis of a Streptomyces griseus relC mutant

Streptomyces relC mutants with an altered ribosomal protein ST-L11 and genetic analysis of a Streptomyces griseus relC mutant

Relationship between synthesis of ribosomes and RNA polymerase in Bacillus subtilis

Alteration of the acidic ribosomal proteins from dormant spores of Bacillus subtilis

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