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Results: 8

1.
Fig. 8

Fig. 8. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Depiction of the pathways considered in the metabolic model for ectoine.

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.
2.
Fig. 2

Fig. 2. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Ectoine synthesis gene organization in H. elongata and other prokaryotes. Shown are the ect genes from the subdivisions of the proteobacteria, the phyla Actinobacteria, Firmicutes, Planctomycetes and Thaumarchaeota. Only ectoine synthesis genes from prokaryotes with known genome sequences are depicted. l-2,4-diaminobutyric acid Nγ-acetyltransferase genes (ectA) are blue, diaminobutyric acid transaminase genes (ectB) are yellow, ectoine synthase (ectC) genes are green, ectoine hydroxylase genes (ectD, ectE) are red and aspartate kinase genes (ask) are pink. The accession numbers of all ect and ask genes are listed in Table S6.

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.
3.
Fig. 3

Fig. 3. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Transcription initiation sites and putative promoters of the ectoine synthesis genes ectABC. Nucleotide sequences of the ectA (A) and ectC (B) promoter regions. Arrows indicate the transcription initiation sites (+ 1), which were mapped by RACE-PCR. The −35 and −10 sequences of the σ70 and σ38 promoters upstream of ectA, and the −24 and −12 sequences of the σ54 promoter upstream of ectC are written in bold. (B) An 18 bp sequence GCCCGCTGACCATT is located at −111 to −128 bp upstream of the ectC transcription initiation site that resembles the consensus sequence of σ54 promoters that are controlled by FleQ (not displayed).

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.
4.
Fig. 4

Fig. 4. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Ectoine-degradation gene organization in H. elongata and other bacteria. Ectoine hydrolase genes (doeA) are blue, Nα-acetyl-l-2,4-diaminobutyric acid deacetylase genes (doeB) are red, genes for AsnC/Lrp-like DNA-binding protein DoeX are pink (doeX), aspartate-semialdehyde dehydrogenase genes (doeC) are green, l-2,4-diaminobutyric acid transaminase genes (doeD) are yellow, eutB (putative threonine dehydratase) are light grey, eutC (putative ornithine cyclodeaminase) are dark grey. The gene doeA and doeB are homologues of eutD and eutE respectively. Only ectoine-degradation genes from bacteria with known genome sequences are depicted. Organisms carrying at least the two genes, doeA and doeB, could only be found in the proteobacteria domain. The accession numbers of all doe genes are listed in Table S6.

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.
5.
Fig. 6

Fig. 6. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Electrophoretic mobility shift assays (EMSA) with DNA-binding protein DoeX.A. EMSA were performed to detect interactions of purified DoeX protein with labelled DNA fragments F1, F2 and F3 located upstream of the doeABX operon.B. In the presence of competitor DNA (500-fold to 1000-fold excess), DoeX specifically binds to fragment F3 resulting in a mobility shift on a non-denaturing polyacrylamide gel. Each assay (20 µl) contained 2 pmol labelled DNA. Lane 0, assay without DoeX protein (control); lane 1, 10 pmol DoeX; lane 2, 20 pmol DoeX; lane 3, 40 pmol DoeX.

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.
6.
Fig. 1

Fig. 1. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Metabolic pathway of the compatible solute ectoine in H. elongata. The degradation pathway is based on genetic and chromatographic analysis carried out in this study. Shown here is the hydrolysis of ectoine that leads directly to Nγ- and Nα-acetyl-l-2,4-diaminobutyric acid. For more details on DoeA activity see text. The depicted ectoine biosynthesis pathway is according to studies previously published (Peters et al., 1990; Göller et al., 1998; Ono et al., 1999). LysC: aspartate kinase; Asd: β-aspartate-semialdehyde-dehydrogenase; EctB: l-2,4-diaminobutyric acid transaminase; EctA: l-2,4-diaminobutyric acid Nγ-acetyltransferase; EctC: ectoine synthase; EctD: ectoine hydroxylase; DoeA: ectoine hydrolase; DoeB: Nα-acetyl-l-2,4-diaminobutyric acid deacetylase; DoeD: l-2,4-diaminobutyric acid transaminase; DoeC: aspartate-semialdehyde dehydrogenase.

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.
7.
Fig. 7

Fig. 7. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Phylogenetic tree of DoeA homologues and their position in the standard phylogeny (‘tree of life’). Branches marked in black correspond to genomes with the same ‘clustered’ organization of the doeAB genes. Red colour is used for those genomes where doeA is located separate from doeB <Ruegeria[previously Silicibacter (Yi et al., 2007)] sp. TM1040, B. xenovorans> or where doeB is not present at all. Organisms considered to be ectoine synthesizers based on the presence of the ectABC genes are boxed in blue. Numbers printed at the nodes are confidence values (varying from 0 to 1) derived from Bayesian statistics. *Oceanobacillus iheyensis carries an ectBC cluster but no ectA.

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.
8.
Fig. 5

Fig. 5. From: A blueprint of ectoine metabolism from the genome of the industrial producer Halomonas elongata DSM 2581T.

Chromatographic analysis of the cytoplasm from (A) E. coli expressing recombinant doeA and (B) H. elongata wild type and ΔdoeB-mutant strain KB42.A. Time course of Nα-Ac-DABA and Nγ-Ac-DABA formation from ectoine in E. coli expressing recombinant doeA. Cells were grown in mineral salt medium containing 340 mM NaCl. Ectoine was added (1 mM) and the cytoplasmic Nα-Ac-DABA (α) and Nγ-Ac-DABA (γ) content was determined by OPA-HPLC shortly before and 20, 40, 60 and 120 min after ectoine was added. Data presented are the mean from two independent experiments. No N-Ac-DABA was formed in E. coli cells without doeA.B. Chromatogram of the cytoplasm from H. elongata KB42 (ΔdoeB) and wild-type cells (WT), which were grown on mineral salt medium (1.03 M NaCl) in the presence of 500 µM glucose and 10 mM ectoine. After depletion of carbon-source glucose, the amino acid content of both strains was determined by OPA-HPLC. In wild-type cells glutamate (glu) and the ectoine precursor Nγ-Ac-DABA (γ) are detectable. In ΔdoeB mutant strain KB42 Nα-Ac-DABA (α) is accumulated as the predominant amino-reactive solute. Similar results were obtained when ectoine degradation was induced by hypoosmotic shock diluting the medium from 1.03 M down to 0.51 M NaCl. A.U., arbitrary units.

Karin Schwibbert, et al. Environ Microbiol. 2011 August;13(8):1973-1994.

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