g glutamate) The pyruvate dehydrogenase also provides acetyl-Co

g. glutamate). The pyruvate dehydrogenase also provides acetyl-CoA used in fatty acid biosynthesis. In addition, the presence of cbbZ in the cbb3 operon is associated with phosphoglycolate phosphatase activity, responsible for removal of phosphoglycolate, an undesirable product of the oxygenase activity of

RubisCO, that must be detoxified preferentially by rechanneling to 3-phosphoglycerate [13, 36]. The co-transcriptional connection between the cbb, pykA and trpEG genes in the cbb3 operon may reflect the substrate requirement www.selleckchem.com/products/Belinostat.html of anthranilate phosphoribosyltransferase for an activated pentose (5-phosphoribosyl 1-pyrophosphate) in order to proceed to the next step of tryptophan biosynthesis [42]. The production of the activated pentose would be stimulated by the activity of the operon. An alternate hypothesis is that the co-transcriptional connection represents a means for pyruvate regeneration since both pykA and trpE/G produce pyruvate. In addition

to the four cbb operons described herein, a fifth gene cluster has recently been detected in A. ferrooxidans that includes genes cbbM, cbbQ3 and cbbO3 predicted to encode form II of RubisCO and its associated chaperons, respectively [43]. The cluster also contains another putative cbbR divergently transcribed from cbbMQO. Future work will evaluate the role of this cluster in CO2 fixation. Acknowledgements This work was supported NVP-HSP990 manufacturer by a grant from Fondecyt 1090451, a Microsoft Sponsored Research Award, a Deutscher Akademischer Austausch

Dienst (DAAD) scholarship to ME, a CONICYT graduate student grant to J-PC and a grant from the Deutsche Forschungsgemeinschaft to BB. Electronic supplementary material Additional file 1: Prediction of secondary structure elements in CbbR of Acidithiobaillus ferrooxidans. Above: secondary structure predictions of alpha-helix, beta-sheet, HTH DNA binding domain, oligomerization domain and LysR-substrate like domain. Below: alignment of amino acid sequences from the HTH domain from several bacteria (abbreviations used can be found in Additional File 2) with the pfam domain00126. (PDF 65 KB) Additional file 2: Alignment and conservation Vorinostat solubility dmso of DNA sequences in the intergenic regions between cbbR and cbbL1 in autotrophic bacteria. The DNA sequences contain the cbb control elements including the operator, the operon promoter (pcbbL) and the promoter cbbR (pcbbR). The CbbR regulator bind to region R (recognition site) and the region A (activation site) of the cbb operator. The nucleotides conserved (TNA-N7/8-TNA, T-N11-A) for to bind CbbR are located in intergenic regions RI-1, RI-2 and RI-3. The prediction of the promoter and the sites for to bind σ70 are in the Selleck NCT-501 columns (sequences -35 and -10).

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