Structure and positioning of three transmembrane segments from Slc11a1 in SDS micelles

Abstract

Slc11a1 is an integral membrane protein with 12 predicted transmembrane domains(TM). In the present work, the secondary structures and positioning of the peptides associated with Slc11a1-TM2, TM3 and TM4(wild-type peptides and functional mutants) in sodium dodecyl sulfate(SDS) were analyzed using circular dichroism(CD) and fluorescence techniques. The results indicate that TM3 is significantly different in secondary structure and topology from TM2 and TM4 in SDS. The peptide TM3 is less structured and is embedded in the SDS less deeply than TM2 and TM4 at pH=4, 5.5 and 7. In addition, the position of TM3 is remarkably shifted towards the direction of the SDS surface with increasing pH, whereas the locations of TM2 and TM4 in SDS are less affected by pH. The E139A substitution in TM3 significantly impairs the pH dependence of the buried depth of TM3 and causes a decrease in helicity in SDS at the three pH values. The G169D mutation has little effect on the topological arrange-ment of TM4 in SDS. In contrast, TM2 and TM4 are topologically similar.

Keywords

Slc11a1 / Transmembrane domain / Positioning / Sodium dodecyl sulfate(SDS) / Circular dichroism(CD)

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