ABCMdb

ABCC7 p.Glu217Val

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Publications

PMID: 19181854 [PubMed] Rath A et al: "Detergent binding explains anomalous SDS-PAGE migration of membrane proteins."

No. Sentence Comment

42 We noted that certain hairpins ran as more diffuse bands than others (e.g., P205S and Q220W vs. V232K and E217V, see Fig. 1B). Login to comment
62 V232D, V232A, P205S, and Q220W) migrated as WT within statistical significance; 2 were faster (V232D and V232K); and 4 were slower (G228L, E217V, E217F, and E217S/S222E). Login to comment
85 Gel shifts, SDS binding, helicity, and column MW of TM3/4 hairpins Hairpin* Gel shift (dMW, %) Bound SDS (g/g) Helicity (MRE X 103)† Column MW (mut-wt, %)‡ V232Dcf -11 Ϯ 2.6 3.4 Ϯ 0.9 -17 Ϯ 1.2 ϩ19 Ϯ 1.5 V232K -10 Ϯ 3.0 3.8 Ϯ 0.6 -16 Ϯ 1.1 ϩ5.6 Ϯ 1.6 A204L -2.2 Ϯ 2.3 6.0 Ϯ 0.7 -18 Ϯ 1.3 ϩ3.4 Ϯ 1.6 P205A/V232Dcf ϩ0.12 Ϯ 5.2 4.7 Ϯ 0.4 -19 Ϯ 2.6 ϩ21 Ϯ 0.6 WT ϩ0.42 Ϯ 4.5 5.4 Ϯ 1.4 -18 Ϯ 2.2 0.0 Ϯ 0.79 V232A ϩ3.6 Ϯ 3.7 5.2 Ϯ 0.4 -18 Ϯ 0.9 ϩ6.1 Ϯ 1.9 P205Scf ϩ4.7 Ϯ 6.0 4.7 Ϯ 1.0 -18 Ϯ 0.7 ϩ4.4 Ϯ 1.6 Q220W ϩ6.3 Ϯ 2.4 5.0 Ϯ 0.7 -21 Ϯ 2.7 -4.9 Ϯ 1.3 G228L ϩ14 Ϯ 5.1 6.9 Ϯ 1.4 -23 Ϯ 1.7 ϩ14 Ϯ 2.6 E217V ϩ28 Ϯ 1.3 6.7 Ϯ 1.0 -25 Ϯ 1.7 ϩ32 Ϯ 4.0 E217F ϩ29 Ϯ 2.8 9.4 Ϯ 1.9 -28 Ϯ 2.6 ϩ17 Ϯ 1.1 E217S/S222E ϩ29 Ϯ 7.6 10 Ϯ 2.3 -25 Ϯ 2.8 ϩ35 Ϯ 0.9 Glycophorin§ - 3.4 Ϯ 0.6 -9.5 Ϯ 1.2 ϩ83 Ϯ 5.1 *Mutant hairpins are listed in order of increasing gel shift. Login to comment

PMID: 22779403 [PubMed] Nadeau VG et al: "Sequence hydropathy dominates membrane protein response to detergent solubilization."

No. Sentence Comment

87 The intensity of mean residue ellipticity at 222 nm, for example, ranged by ~20 000 deg cm2 dmol-1 among the hairpin sequences (compare E217V and V232D, Figure 2A, left), a result that might not initially be anticipated for a "mild" detergent. Login to comment
89 We further noted that the spectra of mutant hairpins solubilized in DDM exhibited a gradation of intensities, whereas SDS-solubilized mutant spectra could be divided into "low helicity" (WT, V232D, A204L, and P205S) or "high helicity" (E217V, ES/SE, and E217F) clusters. Login to comment
96 The correlation of hydropathy levels in TM3/4 mutants and helicity in both detergents was also apparent in the rank ordering of mutants according to their molar residue ellipticity at 222 nm (Figure 2, right), with the exception of three mutants: E217F, E217V, and ES/SE (Figure 2A). Login to comment
144 In DDM (Figure 4B, left), we found that the P205S (E:M = 0.87 ± 0.20), E217V (E:M = 0.78 ± 0.06), E271F (E:M = 0.76 ± 0.12) and A204L spectra (E:M = 0.69 ± 0.02) each displayed excimer fluorescence, and the E:M ratio of each of these "compact" mutants was statistically distinct from the negative control in DDM (E:M = 0.52 ± 0.02, 4.7 × 10-6 ≤ p ≤ 0.008). Login to comment
146 In contrast, after SDS solubilization (Figure 4B, right), excimer emission above negative control (E:M = 0.21 ± 0.004) levels was present only in the A204L mutant (E:M = 0.32 ± 0.06, p = 0.027); the E217V mutant had an E:M ratio higher than the negative control, but this difference was of marginal significance (E:M = 0.28 ± 0.04, p = 0.062). Login to comment
169 A further observation from the sets of CD curves shown in Figure 2 is that the spectra in SDS display ellipticity notably skewed toward the 208 nm lobe, while corresponding spectra in DDM generally have approximately equal ellipticity for the 208 and 222 nm lobes (exception: the loop-based E217V mutant). Login to comment
189 We were thus excited to observe that solubilization by DDM supports a distance <10 Å between pyrene molecules conjugated at the ends of TM3 and TM4, giving rise to a subset of "compact" mutants (P205S, E217V, E217F, and A204L) (Figure 4B, left). Login to comment
193 Consistent with this possibility, the "high helicity" group of SDS-solubilized mutants (E217F, E217V, and ES/SE) has E:M ratios that do not exceed the negative control. Login to comment