Genomic comparison of anoxybacillus flavithermus AK1, a thermophilic bacteria, with other strains.

From ecological and industrial perspectives, Anoxybacillus flavithermus species that lives in a thermophilic environment, are extremely important bacteria due to their potential in producing highly interesting compounds and enzymes. In order to understand the genetic makeup of these thermophiles, we have performed a comparative genomics study of 12 genome-sequenced strains of Anoxybacillus flavithermus bacteria. The genome size of Anoxybacillus flavithermus strains is from 2.5Mbp to 3.7Mbp and on average containing a low percentage of G + C genomic content (˜41.9%). We show that, on the basis of the total gene-content, Anoxybacillus flavithermus strains are grouped in three different subgroups. In the future, it would be interesting to explore these strain subgroups to further understand the lifestyle of thermophilic bacteria. Focussing on the Anoxybacillus flavithermus AK1 strain, which was isolated from a Hot Spring in Saudi Arabia and closely related to A. flavithermus NBRC strain, we identified a unique list of 75 genes specific to AK1 strain, of which 63 of them have homologs in other taxonomically related species. We speculate that these AK1-specific genes might be resulted due to horizontal gene transfer from other bacteria in order to adapt to the extreme environmental conditions. Moreover, we predicted three potential secondary metabolite gene clusters in the AK1 strain that further need to be experimentally characterised. Genomic annotation, secondary metabolite gene clusters and outcomes of the strain genomic comparisons from this study would be the basis for the strain-specific mathematical model for exploiting the metabolism for the industrial and ecological applications.

Insights into Brevibacillus borstelensis AK1 through Whole Genome Sequencing: A Thermophilic Bacterium Isolated from a Hot Spring in Saudi Arabia.

Brevibacillus borstelensis AK1 is a thermophile which grows between the temperatures of 45°C and 70°C. The present study is an extended genome report of B. borstelensis AK1 along with the morphological characterization. The strain is isolated from a hot spring in Saudi Arabia (southeast of the city Gazan). It is observed that the strain AK1 is rod-shaped, motile, and strictly aerobic bacterium. The whole genome sequence resulted in 29 contigs with a total length of 5,155,092 bp. In total, 3,946 protein-coding genes and 139 RNA genes were identified. Comparison with the previously submitted strains of B. borstelensis strains illustrates that strain AK1 has a small genome size but high GC content. The strain possesses putative genes for degradation of a wide range of substrates including polyethylene (plastic) and long-chain hydrocarbons. These genomic features may be useful for future environmental/biotechnological applications.

Genome Sequence of Anoxybacillus flavithermus Strain AK1, a Thermophile Isolated from a Hot Spring in Saudi Arabia.

Anoxybacillus flavithermus strain AK1 was isolated from Al-Ain Alhara, a thermal hot spring located 50 km southeast of the city of Gazan, Saudi Arabia (16°56'N, 43°15'E). The sequenced and annotated genome is 2,630,664 bp and encodes 2,799 genes.

Draft Genome Sequences of Staphylococcus aureus AMRF1 (ST22) and AMRF2 (ST672), Ocular Methicillin-Resistant Isolates.

Sequence type 22 (ST22) and ST672 are the two major emerging clones of community-acquired methicillin-resistant Staphylococcus aureus in India. ST672 strains were found to cause severe ocular infections. We report the draft genome sequences of two emerging strains of methicillin-resistant S. aureus, AMRF1 (ST22) and AMRF2 (ST672), isolated from patients with ocular infections.

Draft Genome Sequence of an Invasive Multidrug-Resistant Strain, Pseudomonas aeruginosa BK1, Isolated from a Keratitis Patient.

Pseudomonas aeruginosa infections are difficult to treat due to the presence of a multitude of virulence factors and antibiotic resistance. Here, we report the draft genome sequence of P. aeruginosa BK1, an invasive and multidrug-resistant strain, isolated from a bacterial keratitis patient in southern India.

Draft Genome Sequence of a Highly Flagellated, Fast-Swimming Archaeon, Methanocaldococcus villosus Strain KIN24-T80 (DSM 22612).

We report the draft genome sequence of a hyperthermophilic Methanocaldococcus villosus strain, KIN24-T80. The gene associated with its heavy flagellum formation was annotated in the 1.2-Mb draft genome sequence, and this strain may be a good model system to study the extensive functional role of flagella and their fast motor activity.

ArhGAP9, a novel MAP kinase docking protein, inhibits Erk and p38 activation through WW domain binding.

We have identified human ArhGAP9 as a novel MAP kinase docking protein that interacts with Erk2 and p38alpha through complementarily charged residues in the WW domain of ArhGAP9 and the CD domains of Erk2 and p38alpha. This interaction sequesters the MAP kinases in their inactive states through displacement of MAP kinase kinases targeting the same sites. While over-expression of wild type ArhGAP9 caused MAP kinase activation by the epidermal growth factor receptor (EGFR) to be suppressed and preserved the actin stress fibres in quiescent Swiss 3T3 fibroblasts, over-expression of an ArhGAP9 mutant defective in MAP kinase binding restored EGFR-induced MAP kinase activation and resulted in significant disruption of the stress fibres, consistent with the role of Erk activation in disassembly of actin stress fibres. The interaction between ArhGAP9 and the MAP kinases represents a novel mechanism of cross-talk between Rho GTPase and MAP kinase signaling.

Crystal structure of AmyA lacks acidic surface and provide insights into protein stability at poly-extreme condition.

Here we report the first crystal structure of a protein, AmyA, a secretory alpha-amylase isolated from Halothermothrix orenii, which is both halophilic and thermophilic. The crystal structure was determined at 1.6 A resolution. AmyA lacks the conserved acidic surface, which is considered essential for protein stability at high salinity. Sedimentation velocity and CD experiments on AmyA reveal the formation of unique reversible poly-dispersed oligomers that show unusually high thermal stability. These studies provide valuable insight into the structural elements that contribute to the stability of AmyA at both physical and chemical extremes and their functional implications.