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The DpsA-homologue of the archaeon Halobacterium salinarum is a ferritin
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2002An iron-rich protein, DpsA(Hsal), was isolated from the archaeon Halobacterium salinarum sharing a sequence identity of 35% with the starvation-induced DNA-binding protein, DpsA, of Synechecoccus sp. PCC7942. It consists of 20-kDa subunits forming a dodecameric structure.
Sabine, Reindel +3 more
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Investigations of iron uptake in Halobacterium salinarum
Biochemical Society Transactions, 2002The iron transport in the extremely halophilic Euryarchaeon Halobacterium salinarum JW5 was investigated. Experiments to detect endogenous siderophores from H. salinarum failed, but it was able to utilize exogenous siderophores. Measurement of the uptake of 55Fe and [14C]citrate gave evidence only for the accumulation of iron.
D, Hubmacher +2 more
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The Low Molecular Weight Proteome of Halobacterium salinarum
Journal of Proteome Research, 2007Systematic investigation of low molecular weight proteins (LMW, below 20 kDa) in the archaeon Halobacterium salinarum resulted in a 6-fold enhancement of the identification rate, reaching 35% of the theoretical proteome in that size range. This was achieved by optimization of common protocols for protein analysis with general applicability.
Klein, C. +12 more
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Isotopic Labeling of Proteins in Halobacterium salinarum
2015It is often necessary to obtain isotopically labeled proteins containing (15)N, (13)C, or (2)H for nuclear magnetic resonance; and (2)H for small-angle neutron scattering or neutron diffraction studies. To achieve uniform isotopic labeling, protein expression is most commonly performed in Escherichia coli or yeast using labeled media. However, proteins
Thomas E, Cleveland, Zvi, Kelman
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On the multicomponent nature of Halobacterium salinarum flagella
Microbiology, 2007Filaments of the flagellum of the halophilic archaeon Halobacterium salinarum consist of five flagellins: A1, A2, B1, B2, and B3, which are encoded by five genes localized in tandem in two flgA and flgB operons. While the role of flagellins A1 and A2 has been determined, the role of the proteins, B operon products, is still unclear.
S. N. Beznosov +2 more
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A microprobe analysis of inorganic elements in Halobacterium salinarum
Cell Biology International, 2005AbstractHalobacterium salinarum were grown on peptone agar containing 4.28 M NaCl, 0.036 M K and other salts. Stationary phase organisms were lifted onto carbon planchets, freeze‐dried, carbon coated and examined in a scanning electron microscope equipped with an X‐ray spectrometer.
Milton B, Engel, Hubert R, Catchpole
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Proteomanalysen an Halobacterium salinarum
2005Im Rahmen dieser Arbeit wurden verschiedene Proteome von H. salinarum untersucht, die nach zellulären Kompartimenten unterschieden wurden in (1) das Flagellarmotor-Proteom (2) das Cytosolproteom und (3) das Membranproteom. Die Untersuchung des Flagellarmotors erfolgte hauptsächlich auf struktureller Basis mittels Elektronenmikroskopie.
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Effects of divalent cations on Halobacterium salinarum cell aggregation
Journal of Bioscience and Bioengineering, 2007Ca(2+) was found to be essential for initiating Halobacterium salinarum CCM 2090 cell aggregation. The floc formed from such aggregation could easily be dissociated without cellular lysis by sodium citrate. Cr(2+), Mn(2+), Fe(3+), Co(2+), Ni(2+), Cu(2+), and Zn(2+) could replace Ca(2+). However, Mg(2+), Sr(2+), Mo(2+), Cd(2+), Sn(2+), Hg(2+), and Pb(2+)
Yoshitaka, Kawakami +3 more
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Flagellar Rotation in the Archaeon Halobacterium salinarum Depends on ATP
Journal of Molecular Biology, 2008Halobacterium salinarum swims with the help of a polarly inserted flagellar bundle. In energized cells, the flagellar motors rotate continuously, occasionally switching the rotational sense. Starving cells become immotile as the energy level drops. Presumably, there is a threshold of energy required for flagellar rotation.
Streif, S. +3 more
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[Multicomponent nature of Halobacterium salinarum flagella].
Mikrobiologiia, 2008Filaments of the flagellum of the halophilic archaeon Halobacterium salinarum consist of five flagellins: A1, A2, B1, B2, and B3, which are encoded by five genes localized in tandem in twoflgA and flgB operons. While the role of flagellins A1 and A2 has been determined, the role of the proteins, B operon products, is still unclear. A mutant strain of H.
S N, Beznosov +2 more
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