The missing lynx of Eurasia at its Southern edge: a connection to the critically endangered Balkan lynx.

The populations of Eurasian lynx in Anatolia are as fragmented as the European populations. Although the origins of and the connections between the European lynx populations have been elucidated, there have been no genetic studies on the lynx populations in Turkey. The lack of genetic and evolutionary information about lynx in Anatolia, which is considered to be a biodiversity hotspot, makes it difficult to track the migration routes during the Quaternary. In this study, we present the genetic characteristics of two isolated lynx populations in Southwest Taurus Mountains and the Turkish Caucasus as well as two individuals from Erzincan area. DNA purified from the ecological scat samples collected from Çiglikara Nature Reserve in Elmali-Antalya and Allahuekber Mountains in Sarikamis-Kars, as well as two roadkill samples from Erzincan, has been analysed for phylogenetic markers such as the mitochondrial DNA control region and cytochrome b. The DNA sequences were compared with haplotypes previously detected in populations from Europe and the Caucasus in order to determine the evolutionary relationships of the populations. This study compares the current genetic structure of some of the Turkish lynx populations to the other lynx genetic data, mostly carried out with museum samples around the world. Three haplotypes were found in three different regions of Anatolia. The Northeast and Southwest populations harbour genetically distinct haplotypes, the latter one, a new haplotype: H13-TR is the only phylogenetic connection to the critically endangered Balkan lynx yet to be described.

Bd oxidase homologue of photosynthetic purple sulfur bacterium Allochromatium vinosum is co-transcribed with a nitrogen fixation related gene.

Purple sulfur bacteria, which are known to be the most ancient among anoxygenic phototrophs, play an important role in the global sulfur cycle. Allochromatium vinosum oxidizes reduced sulfur compounds such as hydrogen sulfide, elemental sulfur and thiosulfide. At low oxygen concentrations, A. vinosum can grow chemotrophically using oxygen as the terminal electron acceptor. Being also a nitrogen fixer, A. vinosum is faced with the paradox of co-existence of aerobic metabolism and nitrogen fixation. Due to growth difficulties, only a few studies have dealt with the aerobic metabolism of the organism and, until now, there has been no information about the genes involved in the respiratory metabolism of purple sulfur bacteria. In this article we show the first terminal oxidase gene for A. vinosum. The presence of a Bd type of quinol oxidase is necessary to protect nitrogenases against the inhibitory effects of oxygen. In this case, a nitrogen fixation related gene is part of the cyd operon and this gene is co-transcribed with cydAB genes. Bd oxidase of A. vinosum may be the earliest form of oxidase where the function of the enzyme is to scavenge the contaminant oxygen during nitrogen fixation. This may be an important clue about the early evolution of oxygenic photosynthesis, perhaps as a protective mechanism for nitrogen fixation.

Expression and functional analysis of glutamate synthase small subunit-like proteins from archaeon Pyrococcus horikoshii.

Glutamate synthase, glutamine α-ketoglutarate amidotransferase (often abbreviated as GOGAT) is a key enzyme in the early stages of ammonia assimilation in bacteria, algae and plants, catalyzing the reductive transamidation of the amido nitrogen from glutamine to α-ketoglutarate to form two molecules of glutamate. Most bacterial glutamate synthases consist of a large and small subunit. The genomes of three Pyrococcus species harbour several open reading frames which show homology with the small subunit of glutamate synthase. There are no open reading frames which may be coding for a large subunit responsible for the glutamate formation in these pyrococcal genomes. In this work, two open reading frames PH0876 and PH1873 from P. horikoshii were cloned and expressed in Escherichia coli as soluble proteins. Both proteins show NADPH-dependent oxidoreductase activity using artificial electron acceptors iodonitrotetrazolium chloride at thermophilic conditions. It is possible that these open reading frames are the products of gene duplication and that they are the early forms of an electron transfer domain in archaea which may have later contributed to many electron transfer enzymes.

Semi-anaerobic growth conditions are favoured by some Escherichia coli strains during heterologous expression of some archaeal proteins.

Host cell physiology is known to play a crucial role in the expression of foreign genes in heterologous systems. Expression of archaeal genes in anaerobic or semi-anaerobic growth conditions of E. coli has been previously reported to be a means of improving solubility of some proteins. Here, we report that some of the Rosetta strains of E. coli, which harbour the rare tRNA genes for the expression of archaeal genes, favour semi-anaerobic conditions for the expression of putative FMN binding domain of glutamate synthase from Methanocaldococcus jannaschii at low inducer concentrations.