Phototrophic Bacteria that Form Heat Resistant Endospores

Ormerod, John G.; Nesbakken, Tore; Torgersen, Yngve

doi:10.1007/978-94-009-0511-5_842

Cited by 10 publications

(8 citation statements)

References 6 publications

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“…Sporomusa [10]. Interestingly, endospore formation in at least some heliobacteria has been documented [11], in keeping with these conclusions. However, it has been claimed that the degree of rRNA sequence similarity between heliobacteria and representative Gram-positive bacteria is actually similar to that between heliobacteria and cyanobacteria [12].…”

Section: Introductionsupporting

confidence: 64%

“…These results therefore provide independant evidence for the phylogenetic relationship between heliobacteria and Gram-positive bacteria. Some heliobacterial properties such as the formation of endospores containing dipicolinic acid [11], their obligately anaerobic nature 11 and some aspects of their enzymology [7] suggest similarities with the clostridia and related bacteria, as predicted by 16S rRNA sequence comparisons, and it will be interesting to see how many other phenotypic characteristics also turn out to be similar.…”

Section: Glycinementioning

confidence: 99%

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Gram-positive cell wall structure of the A3Î³ type in heliobacteria

Pickett

Weiss

Kelly

1994

FEMS Microbiology Letters

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The amino acid composition and structure of the peptidoglycan from Heliobacillus mobilis was determined by one- and two-dimensional thin-layer chromatography of completely and partially hydrolysed cell wall preparations. The structure was found to be of the A3 gamma type, with L,L-diaminopimelate in position 3, D-alanine in position 4 and a glycine interpeptide bridge, as found in certain groups of Gram-positive bacteria including Clostridium perfringens and Nocardioides simplex. The presence of a Gram-positive type of cell wall in heliobacteria is consistent with their phylogenetic relationship to the 'low G + C' Gram-positive bacteria, as previously demonstrated by 16S rRNA sequencing.

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Section: Introductionsupporting

confidence: 64%

Section: Glycinementioning

confidence: 99%

Gram-positive cell wall structure of the A3Î³ type in heliobacteria

Pickett

Weiss

Kelly

1994

FEMS Microbiology Letters

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“…Sporulation in heliobacteria was ¢rst observed during isolation and characterization of Heliobacterium gestii. Initial cultures of H. gestii formed phase-bright structures containing high levels of Ca 2 and dipicolinic acid [12,17]; the latter compound is unique to endospores [18,19]. However, now that H. gestii has been in culture for over 10 years, it rarely sporulates (Madigan, unpublished results).…”

Section: Introductionmentioning

confidence: 99%

Molecular evidence that the capacity for endosporulation is universal among phototrophic heliobacteria

Kimble-Long

2001

FEMS Microbiology Letters

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Although enrichment cultures for anoxygenic phototrophic heliobacteria commonly contain sporulating cells, once strains of heliobacteria are obtained in pure culture, they all but cease to sporulate. In fact, some species of heliobacteria have never been observed to sporulate. Thus, despite their phylogenetic connection to endospore-forming bacteria, the question of sporulation capacity in heliobacteria remains open. We have investigated this problem using PCR and Southern hybridization as tools and show here that all recognized species of heliobacteria tested, as well as several unclassified strains, contain homologs to the ssp genes of Clostridium and Bacillus species, genes that encode key sporulation-specific proteins. It can therefore be concluded that as a group, heliobacteria are likely all to be endosporeforming bacteria in agreement with their phylogenetic placement within the`low GC' Gram-positive bacteria. ß

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“…are phylogenetically related to the gram-positive eubacteria (38), and recently it has been reported that some species form endospores (21).…”

mentioning

confidence: 99%

Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, and Heliobacterium gestii: purification, characterization, and investigation of dinucleotide binding by dehydrogenases by use of empirical methods of protein sequence analysis

1992

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Malate dehydrogenase (MDH; EC 1.1.1.37) from strain NCIB 8327 of the green sulfur bacterium Chlorobium vibrioforme was purified to homogeneity by triazine dye affinity chromatography followed by gel filtration. Purification of MDH gave an approximately 1,000-fold increase in specific activity and recoveries of typically 15 to 20%. The criteria of purity were single bands on sodium dodecyl sulfate (SDS) and nondenaturing polyacrylamide electrophoresis (PAGE) and the detection of a single N terminus in an Edman degradation analysis. MDH activity was detected in purified preparations by activity staining of gels in the direction of malate oxidation. PAGE and gel filtration (Sephadex G-100) analyses showed the native enzyme to be a dimer composed of identical subunits both at room temperature and at 4 degrees C. The molecular weight of the native enzyme as estimated by gel filtration was 77,000 and by gradient PAGE was 74,000. The subunit molecular weight as estimated by SDS-gradient PAGE was 37,500. N-terminal sequences of MDHs from C. vibrioforme, Chlorobium tepidum, and Heliobacterium gestii are presented. There are obvious key sequence similarities in MDHs from the phototrophic green bacteria. The sequences presented probably possess a stretch of amino acids involved in dinucleotide binding which is similar to that of Chloroflexus aurantiacus MDH and other classes of dehydrogenase enzymes but unique among MDHs.

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Phototrophic Bacteria that Form Heat Resistant Endospores

Cited by 10 publications

References 6 publications

Gram-positive cell wall structure of the A3Î³ type in heliobacteria

Gram-positive cell wall structure of the A3Î³ type in heliobacteria

Molecular evidence that the capacity for endosporulation is universal among phototrophic heliobacteria

Malate dehydrogenase from Chlorobium vibrioforme, Chlorobium tepidum, and Heliobacterium gestii: purification, characterization, and investigation of dinucleotide binding by dehydrogenases by use of empirical methods of protein sequence analysis

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