ABCB1 p.Lys380Arg
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PMID: 15182191
[PubMed]
Steinfels E et al: "Characterization of YvcC (BmrA), a multidrug ABC transporter constitutively expressed in Bacillus subtilis."
No.
Sentence
Comment
121
It is shown here that ATP hydrolysis is required to fulfill the Hoechst transport since a YvcC mutant, which was altered in the Walker A-motif (K380R) and therefore deficient in ATP hydrolysis (ATPase activity of the K380R mutant <3% of that of the wild-type protein), was unable to carry out such a transport (Figure 4A).
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ABCB1 p.Lys380Arg 15182191:121:144
status: NEWX
ABCB1 p.Lys380Arg 15182191:121:217
status: NEW132 When AMPPNP was used instead of ATP, no transport activity was observed with wild-type YvcC, and likewise the YvcC K380R mutant was unable to carry out drug transport in the presence of ATP.
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ABCB1 p.Lys380Arg 15182191:132:115
status: NEW183 Panel A: Inverted-membrane vesicles (200 µg) containing either wild-type YvcC (wt) or the K380R YvcC mutant (K380R) were added to the cuvette and after ~1 min incubation at 37 °C, 2 µM Hoechst 33342 was added.
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ABCB1 p.Lys380Arg 15182191:183:95
status: NEWX
ABCB1 p.Lys380Arg 15182191:183:114
status: NEW192 or C41(DE3) bacteria overexpressing either wild-type YvcC (wt) or the K380R YvcC mutant (K380R) were used, and the 7-amino- actinomycin D transport was monitored at 37 °C. After addition of 10 µM 7-aminoactinomycin D (1-2 min), 2 mM ATP or 2 mM AMPPNP was added where indicated by the arrow.
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ABCB1 p.Lys380Arg 15182191:192:70
status: NEWX
ABCB1 p.Lys380Arg 15182191:192:89
status: NEW