ABCC1 p.Gly392Ala
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PMID: 20624916
[PubMed]
Morino M et al: "Single site mutations in the hetero-oligomeric Mrp antiporter from alkaliphilic Bacillus pseudofirmus OF4 that affect Na+/H+ antiport activity, sodium exclusion, individual Mrp protein levels, or Mrp complex formation."
No.
Sentence
Comment
185
MrpC-G82I and MrpA-G392R (Group 3) were the sites of the identified original mutations, which led to the non-alkaliphilic phenotype in B. halodurans C-125.
X
ABCC1 p.Gly392Ala 20624916:185:139
status: NEW190 Neither of the two glycines that were mutated in the original B. halodurans C-125 mutagenesis is crucial for antiport inasmuch as the MrpA-G392A and MrpC-G82P mutants of B. pseudofirmus OF4 yielded mutant Mrp systems with no functional phenotype of significance and only a partial reduction in the membrane levels of MrpC itself for the MrpC-G82P mutant (see Group 8).
X
ABCC1 p.Gly392Ala 20624916:190:139
status: NEW220 Group 8 contains the remaining mutations: MrpA-Y136A, MrpA-H230A, MrpA-W232A, MrpA- Y258A, MrpA-H345A, MrpA-G392A, MrpA-F405A, MrpB-H34A, MrpC-G82P, MrpD-F135A, MrpD-F136A, MrpD-F136E, MrpD-F136T, MrpD- W228A, MrpE-P114A, and MrpF- P28G.
X
ABCC1 p.Gly392Ala 20624916:220:108
status: NEW215 Group 8 contains the remaining mutations: MrpA-Y136A, MrpA-H230A, MrpA-W232A, MrpA-Y258A, MrpA-H345A, MrpA-G392A, MrpA-F405A, MrpB-H34A, MrpC-G82P, MrpD-F135A, MrpD-F136A, MrpD-F136E, MrpD-F136T, MrpD-W228A, MrpE-P114A, and MrpF-P28G.
X
ABCC1 p.Gly392Ala 20624916:215:107
status: NEW