Nomenclature Abstract for Tetragenococcus halophilus halophilus (Mees 1934) Justé et al. 2012.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
George M Garrity
Keyword(s):  
Tetragenococcus Halophilus

scholarly journals Structural and Functional Conversion of Molecular Chaperone ClpB from the Gram-Positive Halophilic Lactic Acid Bacterium Tetragenococcus halophilus Mediated by ATP and Stress

2006 ◽  
Vol 188 (23) ◽  
pp. 8070-8078 ◽  
Author(s):  
Shinya Sugimoto ◽  
Hiroyuki Yoshida ◽  
Yoshimitsu Mizunoe ◽  
Keigo Tsuruno ◽  
Jiro Nakayama ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacterium ◽  
Molecular Chaperone ◽  
Thermal Inactivation ◽  
Gel Filtration ◽  
Ring Structure ◽  
Stress Conditions ◽  
Gel Filtration Chromatography ◽  
Gram Positive ◽  
Tetragenococcus Halophilus

ABSTRACT In this study, we report the purification, initial structural characterization, and functional analysis of the molecular chaperone ClpB from the gram-positive, halophilic lactic acid bacterium Tetragenococcus halophilus. A recombinant T. halophilus ClpB (ClpB Tha ) was overexpressed in Escherichia coli and purified by affinity chromatography, hydroxyapatite chromatography, and gel filtration chromatography. As demonstrated by gel filtration chromatography, chemical cross-linking with glutaraldehyde, and electron microscopy, ClpB Tha forms a homohexameric single-ring structure in the presence of ATP under nonstress conditions. However, under stress conditions, such as high-temperature (>45°C) and high-salt concentrations (>1 M KCl), it dissociated into dimers and monomers, regardless of the presence of ATP. The hexameric ClpB Tha reactivated heat-aggregated proteins dependent upon the DnaK system from T. halophilus (KJE Tha ) and ATP. Interestingly, the mixture of dimer and monomer ClpB Tha , which was formed under stress conditions, protected substrate proteins from thermal inactivation and aggregation in a manner similar to those of general molecular chaperones. From these results, we hypothesize that ClpB Tha forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a disaggregating chaperone in cooperation with KJE Tha and ATP under poststress conditions.

scholarly journals Comparative genomics of Tetragenococcus halophilus

2017 ◽  
Vol 63 (6) ◽  
pp. 369-372 ◽  
Author(s):  
Ikuko Nishimura ◽  
Yuh Shiwa ◽  
Atsushi Sato ◽  
Tetsuya Oguma ◽  
Hirofumi Yoshikawa ◽  
...  
Keyword(s):  
Comparative Genomics ◽  
Tetragenococcus Halophilus

Co-culture with Tetragenococcus halophilus changed the response of Zygosaccharomyces rouxii to salt stress

2020 ◽  
Vol 95 ◽  
pp. 279-287
Author(s):  
Shangjie Yao ◽  
Rongqing Zhou ◽  
Yao Jin ◽  
Liqiang Zhang ◽  
Jun Huang ◽  
...  
Keyword(s):  
Salt Stress ◽  
Zygosaccharomyces Rouxii ◽  
Tetragenococcus Halophilus

scholarly journals Topology of AspT, the Aspartate:Alanine Antiporter of Tetragenococcus halophilus, Determined by Site-Directed Fluorescence Labeling

2007 ◽  
Vol 189 (19) ◽  
pp. 7089-7097 ◽  
Author(s):  
Kei Nanatani ◽  
Takashi Fujiki ◽  
Kazuhiko Kanou ◽  
Mayuko Takeda-Shitaka ◽  
Hideaki Umeyama ◽  
...  
Keyword(s):  
Three Dimensional ◽  
Amino Acid Sequences ◽  
Fluorescence Labeling ◽  
Dimensional Structure ◽  
Specific Probe ◽  
Cytoplasmic Loop ◽  
Intact Cells ◽  
Tetragenococcus Halophilus ◽  
Substituted Cysteine Accessibility ◽  
And Function

ABSTRACT The gram-positive lactic acid bacterium Tetragenococcus halophilus catalyzes the decarboxylation of l-aspartate (Asp) with release of l-alanine (Ala) and CO2. The decarboxylation reaction consists of two steps: electrogenic exchange of Asp for Ala catalyzed by an aspartate:alanine antiporter (AspT) and intracellular decarboxylation of the transported Asp catalyzed by an l-aspartate-β-decarboxylase (AspD). AspT belongs to the newly classified aspartate:alanine exchanger family (transporter classification no. 2.A.81) of transporters. In this study, we were interested in the relationship between the structure and function of AspT and thus analyzed the topology by means of the substituted-cysteine accessibility method using the impermeant, fluorescent, thiol-specific probe Oregon Green 488 maleimide (OGM) and the impermeant, nonfluorescent, thiol-specific probe [2-(trimethylammonium)ethyl]methanethiosulfonate bromide. We generated 23 single-cysteine variants from a six-histidine-tagged cysteineless AspT template. A cysteine position was assigned an external location if the corresponding single-cysteine variant reacted with OGM added to intact cells, and a position was assigned an internal location if OGM labeling required cell lysis. The topology analyses revealed that AspT has a unique topology; the protein has 10 transmembrane helices (TMs), a large hydrophilic cytoplasmic loop (about 180 amino acids) between TM5 and TM6, N and C termini that face the periplasm, and a positively charged residue (arginine 76) within TM3. Moreover, the three-dimensional structure constructed by means of the full automatic modeling system indicates that the large hydrophilic cytoplasmic loop of AspT possesses a TrkA_C domain and a TrkA_C-like domain and that the three-dimensional structures of these domains are similar to each other even though their amino acid sequences show low similarity.

scholarly journals Genomic insights into the non-histamine production and proteolytic and lipolytic activities of Tetragenococcus halophilus KUD23

2017 ◽  
Vol 365 (1) ◽  
Author(s):  
Jong-Hoon Lee ◽  
Sojeong Heo ◽  
Keuncheol Jeong ◽  
Byunghoon Lee ◽  
Do-Won Jeong
Keyword(s):  
Tetragenococcus Halophilus ◽  
Histamine Production
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