scholarly journals Localization of the ATP-binding cassette (ABC) transport proteins PfMRP1, PfMRP2, and PfMDR5 at the Plasmodium falciparum plasma membrane

2009 ◽  
Vol 8 (1) ◽  
pp. 205 ◽  
Author(s):  
Reginald A Kavishe ◽  
Jeroen MW van den Heuvel ◽  
Marga van de Vegte-Bolmer ◽  
Adrian JF Luty ◽  
Frans GM Russel ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Plasma Membrane ◽  
Transport Proteins ◽  
Atp Binding ◽  
Abc Transport ◽  
Atp Binding Cassette

Improvement of Daptomycin Yield by Overexpression of ATP-Binding Cassette (ABC) Transport Proteins Genes of Daptomycin Gene Cluster

2013 ◽  
Vol 295-298 ◽  
pp. 164-168
Author(s):  
Guang Hai Yu ◽  
Yu Tao Min ◽  
Yuan Sen Hu ◽  
Yan Li Yin ◽  
Liang Huang
Keyword(s):  
Sugar Transport ◽  
Dry Weight ◽  
Transport Proteins ◽  
Reducing Sugar ◽  
Atp Binding ◽  
Positive Role ◽  
Sugar Utilization ◽  
Abc Transport ◽  
Daptomycin Production ◽  
Atp Binding Cassette

The effects of the genes of ORF53-55, which code ATP-binding cassette (ABC) transport proteins, on daptomycin production were investigated by overexpression. The yield of daptomycin was promoted significantly when either of the genes of ORF53, ORF54 or ORF55 was overexpressed individually or by a combined manner. The results above suggested that the ORF53, ORF54 and ORF55 genes had positive cooperativity in the biosynthesis of daptomycin. The dry weight and sugar utilization of HP-ORF53-55 is significantly improved as compared with the LC-54-16. Based on these results, it was speculated that the genes of ORF 53, 54 and 55 may play an important positive role in the process of reducing sugar transport, which enhanced the cell growth and daptomycin biosynthesis.

scholarly journals Two B-type ATP-binding cassette (ABC) transporters localize to the plasma membrane in Thalictrum minus

2015 ◽  
Vol 32 (3) ◽  
pp. 243-247 ◽  
Author(s):  
Nobukazu Shitan ◽  
Kazuyoshi Terasaka ◽  
Hirobumi Yamamoto ◽  
Fumihiko Sato ◽  
Kazufumi Yazaki
Keyword(s):  
Plasma Membrane ◽  
Abc Transporters ◽  
Atp Binding ◽  
Thalictrum Minus ◽  
Atp Binding Cassette

scholarly journals Endocytosis and vacuolar degradation of the plasma membrane-localized Pdr5 ATP-binding cassette multidrug transporter in Saccharomyces cerevisiae.

1995 ◽  
Vol 15 (11) ◽  
pp. 5879-5887 ◽  
Author(s):  
R Egner ◽  
Y Mahé ◽  
R Pandjaitan ◽  
K Kuchler
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Plasma Membrane ◽  
Indirect Immunofluorescence ◽  
Half Life ◽  
Molecular Mechanisms ◽  
Atp Binding ◽  
Multidrug Transporter ◽  
Restrictive Temperature ◽  
Mutant Cells ◽  
Atp Binding Cassette

Multidrug resistance (MDR) to different cytotoxic compounds in the yeast Saccharomyces cerevisiae can arise from overexpression of the Pdr5 (Sts1, Ydr1, or Lem1) ATP-binding cassette (ABC) multidrug transporter. We have raised polyclonal antibodies recognizing the yeast Pdr5 ABC transporter to study its biogenesis and to analyze the molecular mechanisms underlying MDR development. Subcellular fractionation and indirect immunofluorescence experiments showed that Pdr5 is localized in the plasma membrane. In addition, pulse-chase radiolabeling of cells and immunoprecipitation indicated that Pdr5 is a short-lived membrane protein with a half-life of about 60 to 90 min. A dramatic metabolic stabilization of Pdr5 was observed in delta pep4 mutant cells defective in vacuolar proteinases, and indirect immunofluorescence showed that Pdr5 accumulates in vacuoles of stationary-phase delta pep4 mutant cells, demonstrating that Pdr5 turnover requires vacuolar proteolysis. However, Pdr5 turnover does not require a functional proteasome, since the half-life of Pdr5 was unaffected in either pre1-1 or pre1-1 pre2-1 mutants defective in the multicatalytic cytoplasmic proteasome that is essential for cytoplasmic protein degradation. Immunofluorescence analysis revealed that vacuolar delivery of Pdr5 is blocked in conditional end4 endocytosis mutants at the restrictive temperature, showing that endocytosis delivers Pdr5 from the plasma membrane to the vacuole.

scholarly journals Identification and Characterization of SNQ2, a New Multidrug ATP Binding Cassette Transporter of the Yeast Plasma Membrane

1995 ◽  
Vol 270 (30) ◽  
pp. 18150-18157 ◽  
Author(s):  
Anabelle Decottignies ◽  
Laurence Lambert ◽  
Patrice Catty ◽  
Herv Degand ◽  
Eric A. Epping ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Atp Binding ◽  
Yeast Plasma Membrane ◽  
Atp Binding Cassette Transporter ◽  
Identification And Characterization ◽  
Atp Binding Cassette

Broad-spectrum modulation of ATP-binding cassette transport proteins by the taxane derivatives ortataxel (IDN-5109, BAY 59-8862) and tRA96023

2004 ◽  
Vol 53 (5) ◽  
pp. 363-369 ◽  
Author(s):  
Hans Minderman ◽  
Tracy A. Brooks ◽  
Kieran L. O’Loughlin ◽  
Iwao Ojima ◽  
Ralph J. Bernacki ◽  
...  
Keyword(s):  
Broad Spectrum ◽  
Transport Proteins ◽  
Atp Binding ◽  
Atp Binding Cassette

scholarly journals An Operon for a Putative ATP-Binding Cassette Transport System Involved in Acetoin Utilization ofBacillus subtilis

2000 ◽  
Vol 182 (19) ◽  
pp. 5454-5461 ◽  
Author(s):  
Ken-Ichi Yoshida ◽  
Yasutaro Fujita ◽  
S. Dusko Ehrlich
Keyword(s):  
Stationary Phase ◽  
Transport System ◽  
Minimal Medium ◽  
Atp Binding ◽  
Ofbacillus Subtilis ◽  
Abc Transport ◽  
Maximum Cell ◽  
Highly Hydrophobic ◽  
Single Operon ◽  
Atp Binding Cassette

ABSTRACT The ytrABCDEF operon of Bacillus subtiliswas deduced to encode a putative ATP-binding cassette (ABC) transport system. YtrB and YtrE could be the ABC subunits, and YtrC and YtrD are highly hydrophobic and could form a channel through the cell membrane, while YtrF could be a periplasmic lipoprotein for substrate binding. Expression of the operon was examined in cells grown in a minimal medium. The results indicate that the expression was induced only early in the stationary phase. The six ytr genes form a single operon, transcribed from a putative ςA-dependent promoter present upstream of ytrA. YtrA, which possesses a helix-turn-helix motif of the GntR family, acts probably as a repressor and regulates its own transcription. Inactivation of the operon led to a decrease in maximum cell yield and less-efficient sporulation, suggesting its involvement in the growth in stationary phase and sporulation. It is known that B. subtilis produces acetoin as an external carbon storage compound and then reuses it later during stationary phase and sporulation. When either the entireytr operon or its last gene, ytrF, was inactivated, the production of acetoin was not affected, but the reuse of acetoin became less efficient. We suggest that the Ytr transport system plays a role in acetoin utilization during stationary phase and sporulation.

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