Characteristics of maltose transport system in the endosymbiont Chlorella variabilis of Paramecium bursaria

2021 ◽  
Author(s):  
Aika Shibata ◽  
Fumio Takahashi ◽  
Nobutaka Imamura ◽  
Masahiro Kasahara
Keyword(s):  
Transport System ◽  
Paramecium Bursaria ◽  
Maltose Transport ◽  
Chlorella Variabilis

scholarly journals Archaeal Binding Protein-Dependent ABC Transporter: Molecular and Biochemical Analysis of the Trehalose/Maltose Transport System of the Hyperthermophilic Archaeon Thermococcus litoralis

1998 ◽  
Vol 180 (3) ◽  
pp. 680-689 ◽  
Author(s):  
Reinhold Horlacher ◽  
Karina B. Xavier ◽  
Helena Santos ◽  
Jocelyne DiRuggiero ◽  
Marina Kossmann ◽  
...  
Keyword(s):  
Transport System ◽  
Signal Sequence ◽  
Binding Protein ◽  
Inducible Promoter ◽  
Transport Systems ◽  
Thermococcus Litoralis ◽  
Hyperthermophilic Archaeon ◽  
E Coli ◽  
Transmembrane Segments ◽  
Maltose Transport

ABSTRACT We report the cloning and sequencing of a gene cluster encoding a maltose/trehalose transport system of the hyperthermophilic archaeonThermococcus litoralis that is homologous to themalEFG cluster encoding the Escherichia colimaltose transport system. The deduced amino acid sequence of themalE product, the trehalose/maltose-binding protein (TMBP), shows at its N terminus a signal sequence typical for bacterial secreted proteins containing a glyceride lipid modification at the N-terminal cysteine. The T. litoralis malE gene was expressed in E. coli under control of an inducible promoter with and without its natural signal sequence. In addition, in one construct the endogenous signal sequence was replaced by the E. coli MalE signal sequence. The secreted, soluble recombinant protein was analyzed for its binding activity towards trehalose and maltose. The protein bound both sugars at 85°C with aKd of 0.16 μM. Antibodies raised against the recombinant soluble TMBP recognized the detergent-soluble TMBP isolated from T. litoralis membranes as well as the products from all other DNA constructs expressed in E. coli. Transmembrane segments 1 and 2 as well as the N-terminal portion of the large periplasmic loop of the E. coli MalF protein are missing in the T. litoralis MalF. MalG is homologous throughout the entire sequence, including the six transmembrane segments. The conserved EAA loop is present in both proteins. The strong homology found between the components of this archaeal transport system and the bacterial systems is evidence for the evolutionary conservation of the binding protein-dependent ABC transport systems in these two phylogenetic branches.

scholarly journals The Maltose Transport System of Escherichia coli Displays Positive Cooperativity in ATP Hydrolysis

1996 ◽  
Vol 271 (9) ◽  
pp. 4858-4863 ◽  
Author(s):  
Amy L. Davidson ◽  
Sean S. Laghaeian ◽  
Daynene E. Mannering
Keyword(s):  
Escherichia Coli ◽  
Transport System ◽  
Atp Hydrolysis ◽  
Maltose Transport ◽  
Positive Cooperativity

OrbiSIMS Imaging Identifies Molecular Constituents of the Perialgal Vacuole Membrane of Paramecium bursaria with Symbiotic Chlorella variabilis

2019 ◽  
Vol 91 (22) ◽  
pp. 14545-14551 ◽  
Author(s):  
Satoka Aoyagi ◽  
Yuuki Kodama ◽  
Melissa K. Passarelli ◽  
Jean-Luc Vorng ◽  
Tomoko Kawashima ◽  
...  
Keyword(s):  
Paramecium Bursaria ◽  
Vacuole Membrane ◽  
Chlorella Variabilis

scholarly journals Molecular and Biochemical Analysis of MalK, the ATP-hydrolyzing Subunit of the Trehalose/Maltose Transport System of the Hyperthermophilic ArchaeonThermococcus litoralis

1999 ◽  
Vol 274 (29) ◽  
pp. 20259-20264 ◽  
Author(s):  
Gerhard Greller ◽  
Reinhold Horlacher ◽  
Jocelyne DiRuggiero ◽  
Winfried Boos
Keyword(s):  
Transport System ◽  
Biochemical Analysis ◽  
Maltose Transport

Symbiotic Chlorella variabilis strain, 1 N, can influence the digestive process in the host Paramecium bursaria during early infection

Symbiosis ◽  
2016 ◽  
Vol 71 (1) ◽  
pp. 47-55
Author(s):  
Yuuki Kodama ◽  
Miyuki Nagase ◽  
Akane Takahama
Keyword(s):  
Early Infection ◽  
Paramecium Bursaria ◽  
Digestive Process ◽  
Chlorella Variabilis
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