Topic
Methanosarcina barkeri
About: Methanosarcina barkeri is a research topic. Over the lifetime, 703 publications have been published within this topic receiving 32151 citations.
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TL;DR: Similarities between the nitrogen-fixing systems of the archaebacteriumMethanosarcina barkeri and a number of eubacteria were investigated and homology with M. barkeri was demonstrated.
Abstract: Similarities between the nitrogen-fixing systems of the archaebacteriumMethanosarcina barkeri (strain Fusaro) and a number of eubacteria were investigated. Using antibodies againstRhizobium leguminosarum nitrogenase and a probe of clonednif-HDK genes of this species, homology withM. barkeri was demonstrated on the protein level and to a greater extent on the DNA level.
1 citations
Journal Article•
TL;DR: Methanogenic archaea possess unusual seryl-tRNA synthetases (SerRS), evolutionarily distinct from the SerRSs found in other archaea, eucaryotes and bacteria, which presumably precluded the complementation of endogenous SerRS function in both E. coli and S. cerevisiae.
Abstract: Summary Methanogenic archaea possess unusual seryl-tRNA synthetases (SerRS), evolutionarily distinct from the SerRSs found in other archaea, eucaryotes and bacteria. Our recent X-ray structural analysis of Methanosarcina barkeri SerRS revealed an idiosyncratic N-terminal domain and catalytic zinc ion in the active site. To shed further light on substrate discrimination by methanogenic-type SerRS, we set up to explore in vivo the interaction of methanogenic-type SerRSs with their cognate tRNAs in Escherichia coli or Saccharomyces cerevisiae. The expression of various methanogenic-type SerRSs was toxic for E. coli, resulting in the synthesis of erroneous proteins, as revealed by b-galactosidase stability assay. Although SerRSs from methanogenic archaea recognize tRNAs Ser from all three domains of life i nv itro, the toxicity presumably precluded the complementation of endogenous SerRS function in both, E. coli and S. cerevisiae. However, despite the observed toxicity, coexpression of methanogenic-type SerRS with its cognate tRNA suppressed bacterial amber mutation.
1 citations
TL;DR: A type I DNA Topoisomerase from a mesophilic archaebacteria, Methanosarcina barkeri, is identified and the enzyme activity residing in a high molecular mass complex is found to be magnesium-dependent and relaxes negatively supercoiled DNA.
1 citations