Isolation and purification of a substance inducing competence and inactivating transforming DNA in pneumococcus

Kohoutová, M.; Braná, H.; Holubová, I.

doi:10.1016/0006-291x(68)90458-0

Cited by 19 publications

(12 citation statements)

References 9 publications

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“…There is also evidence that donor strains of Escherichia colh produce "recombination stimulating factors" (18) which affect recipients. Transformable streptococci produce competence factors, extracellular proteins required for transformation (19,20). Many fungal sex hormones have been described (for a review see ref.…”

Section: Discussionmentioning

confidence: 99%

Induced cell aggregation and mating in Streptococcus faecalis: evidence for a bacterial sex pheromone.

Dunny¹,

Brown²,

Clewell³

1978

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

508

335

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Recipient strains of Streptococcus faecalis produce a trypsin sensitive, heat resistant, nuclease resistant factor, designated clumping-inducing agent (CIA) which causes strains carrying certain conjugative plasmids to aggregate. RNA and protein synthesis but not DNA synthesis are required for aggregation to occur. Recipient filtrates that contain CIA activity also induce donors to mate at high frequencies. Introduction of a transferable plasmid into strains producing CIA dramatically reduces the amount of CIA activity produced by the strain but allows the strain to respond to exogenously added CIA. Our data suggest that CIA represents a bacterial sex hormone (pheromone).

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Section: Discussionmentioning

confidence: 99%

Induced cell aggregation and mating in Streptococcus faecalis: evidence for a bacterial sex pheromone.

Dunny¹,

Brown²,

Clewell³

1978

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

508

335

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“…All strains were grown in competence media (THY with the addition of 0.2% BSA, 0.2% glucose and 0.02% CaCl 2 , made fresh) until just turbid. Bacteria were then diluted 1:30 in fresh competence media, and 200 ng ml −1 of competence stimulating peptide 1 (Kohoutova et al , 1968; Havarstein et al , 1995) was added together with 100 ng of plasmid DNA. The bacteria were grown at 37°C for an additional 2 h, after which the culture was plated on blood agar containing 0.3 μg ml −1 erythromycin.…”

Section: Methodsmentioning

confidence: 99%

Characterization of the dihydrolipoamide dehydrogenase from Streptococcus pneumoniae and its role in pneumococcal infection

Smith

Roche

Trombe

et al. 2002

Molecular Microbiology

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had an 85% reduction in a-galactosidase activity and showed virtually no transport of galactose into the cells, which can explain these phenotypic changes. The DLDH-negative bacteria produced only 50% of normal capsular polysaccharide, a phenotype that may be associated with impaired carbohydrate metabolism. IntroductionDihydrolipoamide dehydrogenases (DLDH; EC 1.8.1.4) are homodimeric flavoproteins that catalyse the NAD + -dependent reoxidation of dihydrolipoamide (DLA) in a number of multienzyme complexes (Perham et al., 1987;Carothers et al., 1989;Williams, 1992;de Kok et al., 1998). These complexes are primarily involved in the conversion of 2-oxo acids to their corresponding acyl-CoA derivative and are involved in important steps in aerobic and anaerobic metabolism (Carothers et al., 1989;de Kok et al., 1998). DLDH makes up the E3 component of the pyruvate dehydrogenase, 2-oxo glutarate dehydrogenase and branchedchain 2-oxo acid dehydrogenase complexes. Additionally, DLDH functions in the glycine cleavage multienzyme complex (where it is referred to as the L protein), as well as in the acetoin dehydrogenase complex in bacteria such as Bacillus subtilis, Clostridium magnum and Pelobacter carbinolicus (Wieland, 1983;Dietrichs and Andreesen, 1990;Kruger et al., 1994;Oppermann and Steinbuchel, 1994;Berg and de Kok, 1997;de Kok et al., 1998;Aevarsson et al., 1999;Huang et al., 1999).Even though the main function of DLDH is associated with its role in 2-oxo acid dehydrogenase complexes, the fact that DLDH is present in organisms that lack these complexes suggests that the enzyme may have additional functions (Danson et al., 1987;Danson, 1988a). Trypanosoma brucei as well as various archeabacteria exhibit simpler ways of converting 2-oxo acids, while still containing a DLDH enzyme (Danson et al., 1987;Danson, 1988b). This suggests that the DLDH must have a separate function in these organisms, and that this function is possibly retained in species in which the DLDH is also part of a 2-oxo acid dehydrogenase complex. Richarme and Heine (1986) and Richarme (1989) proposed that DLDH may be involved in regulation of the transport of galactose, maltose and ribose across the membrane of SummaryIn the present study, we have characterized the dihydrolipoamide dehydrogenase (DLDH) of Streptococcus pneumoniae and its role during pneumococcal infection. We have also demonstrated that a lack of DLDH results in a deficiency in a-galactoside metabolism and galactose transport. DLDH is an enzyme that is classically involved in the three-step conversion of 2-oxo acids to their respective acyl-CoA derivatives, but DLDH has also been shown to have other functions. The dldh gene was virtually identical in three pneumococcal strains examined. Besides the functional domains and motifs associated with this enzyme, analysis of the pneumococcal dldh gene sequence revealed the presence of an N-terminal lipoyl domain. DLDH-negative bacteria totally lacked DLDH activity, indicating that this gene encodes the only DLDH in S. pneumoniae. The...

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“…(1984) 157, 152-157). Competence factors have been described in Pneumococcus [4,5] and in B. subtilis [6,7]. This buffer stimulates up to 40-50 times the transformation frequency of FB92 and FB94 strains, while it has an inhibitory effect on the other two mutants and on the wild-type strain.…”

Section: Discussionmentioning

confidence: 99%

“…Competence factors have been described in Pneumococcus [4,5] and in B. subtilis [6,7].In a previous paper we described the isolation and characterization of four different B. subtilis mutants altered in competence development. (1984) 157, 152-157).…”

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Effect of potassium phosphate on Bacillus subtilis competence mutants

Mastromei¹

1984

FEMS Microbiology Letters

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We have previously described the isolation and characterization of four Bacillus subtilis competence‐deficient mutants (J. Bacteriol. (1984) 157, 152–157). Further experiments, reported here, have shown that the transformation frequency of two of the mutants (FB92 and FB94) can be increased by the addition of high concentrations of potassium phosphate buffer present in the concentrated supernatant. This buffer stimulates up to 40–50 times the transformation frequency of FB92 and FB94 strains, while it has an inhibitory effect on the other two mutants and on the wild‐type strain. Potassium phosphate inhibits DNA binding to competent cells but, at the same time, activates a second much less efficient binding system which partly restores the capacity of FB92 and FB94 mutants to take up DNA.

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Isolation and purification of a substance inducing competence and inactivating transforming DNA in pneumococcus

Cited by 19 publications

References 9 publications

Induced cell aggregation and mating in Streptococcus faecalis: evidence for a bacterial sex pheromone.

Induced cell aggregation and mating in Streptococcus faecalis: evidence for a bacterial sex pheromone.

Characterization of the dihydrolipoamide dehydrogenase from Streptococcus pneumoniae and its role in pneumococcal infection

Effect of potassium phosphate on Bacillus subtilis competence mutants

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