Methane is a most important greenhouse gas for planetary heating and it’s produced by methanogenic microorganisms as a metabolic byproduct and creates climate change. Methanogens are ancient organisms on earth found in anaerobic environments and methane is a key greenhouse gas concerned with methanogens. Therefore here is intense interest to writing this paper. A number of experiments have already conducted to study the methanogens in various environments such as rumen and intestinal system of animals, fresh water and marine sediments, swamps and marshes, hot springs, sludge digesters, and within anaerobic protozoa which utilize carbon dioxide in the presence of hydrogen and produce methane. The diversity of methanogens, belong to the domain Archaea and get involved in biological production of methane that catalyzes the degradation of organic compound as a part of global carbon cycle called methanogenesis. Majorly in this article we summaries the diversity of methanogens and their impact on global warming.
Archebakterie stanowią bardzo złożoną, a przez to niezwykle interesującą grupę drobnoustrojów, zarówno ze względu na ich uzdolnienia do zasiedlania rozmaitych środowisk, w tym zwłaszcza ekstremalnych, jak również z powodu specyficznej budowy komponentów komórkowych. W ostatnich latach obserwuje się duży rozwój wiedzy na ich temat, co skutkuje pojawieniem się ogromnej puli mniej lub bardziej szczegółowych publikacji. W literaturze polskojęzycznej brakuje jednak prac przeglądowych ujmujących szerzej temat budowy i fizjologii tych organizmów. Niniejsza praca uzupełnia tę lukę, omawiając wybrane elementy komórek Archaea wyróżniające się unikalną budową lub funkcjami, takie jak warstwa S, ściana komórkowa, błona cytoplazmatyczna oraz różnorodne wypustki komórkowe. Ponadto zwrócono uwagę na niektóre niezwykłe aspekty metabolizmu archebakterii.
The haloarchaeal diversity of a salt mine, a natural cave in central Anatolia, was investigated using convential microbiological and molecular biology methods. Eight halophilic archaeal isolates selected based on their colony morphology and whole cell protein profiles were taxonomically classified on the basis of their morphological, physiological, biochemical properties, polar lipid and protein profiles and 16S rDNA sequences. From the 16S rDNA sequences comparisons it was established that the isolates CH2, CH3 and CHC resembled Halorubrum saccharovorum by 98.8%, 98.9% and 99.5%, respectively. There was a 99.7% similarity between the isolate CH11 and Halobacterium noricense and 99.2% between the isolate CHA1 and Haloarcula argentinensis. The isolate CH8K and CH8B revealed a similarity rate of 99.8% and 99.3% to Halococcus dombrowskii, respectively. It was concluded that the isolates named CH2, CH3 and CHC were clustered in the genus Halorubrum and that CHA1 and CH7 in the genus Haloarcula, CH8K and CH8B in the genus Halococcus and CH11 in the genus Halobacterium.
The 2',3'-cyclic phosphate termini are produced, as either intermediates or final products, during RNA cleavage by many different endoribonucleases. Likewise, ribozymes such as hammerheads, hairpins, or the hepatitis delta ribozyme, generate 2',3'-cyclic phosphate ends. Discovery of the RNA 3'-terminal phosphate cyclase has indicated that cyclic phosphate termini in RNA can also be produced by an entirely different mechanism. The RNA 3'-phosphate cyclase converts the 3'-terminal phosphate in RNA into the 2',3'-cyclic phosphodiester in the ATP-dependent reaction which involves formation of the covalent cyclase-AMP and the RNA-Ni3'pp5'A intermediates. The findings that several eukaryotic and prokaryotic RNA ligases require the 2',3'-cyclic phosphate for the ligation of RNA molecules raised a possibility that the RNA 3'-phosphate cyclase may have an anabolic function in RNA metabolism by generating terminal cyclic groups required for ligation. Recent cloning of a cDNA encoding the human cyclase indicated that genes encoding cyclase-like proteins are conserved among Eucarya, Bacteria, and Archaea. The protein encoded by the Escherichia coli gene was overexpressed and shown to have the RNA 3'-phosphate cyclase activity. This article reviews properties of the human and bacterial cyclases, their mechanism of action and substrate specificity. Possible biological functions of the enzymes are also discussed.
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