ABCB1 p.Ser23Ala
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PMID: 15709779
[PubMed]
Kaur P et al: "Biochemical characterization of domains in the membrane subunit DrrB that interact with the ABC subunit DrrA: identification of a conserved motif."
No.
Sentence
Comment
253
These changes include S23A, G25A, E26D, and S35A in the N-terminal domain and C260A and A270S in the C-terminal domain.
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ABCB1 p.Ser23Ala 15709779:253:22
status: NEW254 Doxorubicin resistance assays showed that S23A, G25A, and E26D mutations in the N-terminal domain confer sensitivity to between 4 and 6 µg/mL of doxorubicin while the cells containing the wild-type DrrA and DrrB grow up to 8-10 µg/mL of doxorubicin (Table 2).
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ABCB1 p.Ser23Ala 15709779:254:42
status: NEW257 Protein expression analysis by SDS-PAGE showed that most mutations, except S23A, S35A, and A270Y show varying degrees of reduction in the levels of DrrA and DrrB.
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ABCB1 p.Ser23Ala 15709779:257:75
status: NEW267 Table 2: Doxorubicin Resistance of E. coli N43 Cells Expressing Wild-Type DrrA with DrrB Containing Mutations in the N-Terminal Cytoplasmic Tail or the C-Terminal Enda amt of dox, µg/mLdomain of DrrB location of cysteine 0 4 6 8 (wild type) C260 +++ +++ +++ ++ N-terminus S23A +++ ++ - - N-terminus G25A +++ ( - - N-terminus E26D +++ ( - - N-terminus S35A +++ +++ +++ +++ N-terminus S35I +++ ( - - C-terminus C260A +++ +++ +++ - C-terminus C260E +++ +++ +++ - C-terminus A270S +++ +++ +++ + C-terminus A270Y +++ +++ ++ ++ vector only pSU2718 +++ ( - - a Legend: +++, very good growth; ++ good growth; + some growth; -, no growth.
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ABCB1 p.Ser23Ala 15709779:267:277
status: NEW327 Mutagenesis of certain residues in and around the conserved motif in the N terminus of DrrB, including S23A, G25A, E26D, and S35I, resulted in sensitivity to doxorubicin, although mutagenesis of C260 and A270 in the C terminus did not confer doxorubicin sensitivity significantly.
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ABCB1 p.Ser23Ala 15709779:327:103
status: NEW331 Second-site suppressor analysis of the S23A, G25A, E26D, and S35I mutations will be carried out in the future to verify if these residues are indeed directly involved in interaction with DrrA, as is suggested by the cysteine cross-linking studies reported here.
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ABCB1 p.Ser23Ala 15709779:331:39
status: NEW