TY - JOUR
T1 - BLaTM 2.0, a Genetic Tool Revealing Preferred Antiparallel Interaction of Transmembrane Helix 4 of the Dual-Topology Protein EmrE
AU - Julius, Ayse
AU - Laur, Lisa
AU - Schanzenbach, Christoph
AU - Langosch, Dieter
N1 - Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2017/6/2
Y1 - 2017/6/2
N2 - Parallel and antiparallel transmembrane helix–helix interactions support the folding and non-covalent assembly of many integral membrane proteins. While several genetic tools are currently in use to study parallel transmembrane helix–helix interactions, antiparallel associations have been difficult to determine. Here, we present a novel genetic approach, termed BLaTM 2.0, which can be used in combination with the recently presented BLaTM 1.2 to compare the efficiency of antiparallel and parallel transmembrane domain (TMD) interactions in a natural membrane. In a practical application of the BLaTM system, we find that the antiparallel interaction of TMD4, the known dimerization domain of the dual-topology small multidrug transporter EmrE, is sequence-specific and much stronger than the parallel one. This suggests that TMD4 has evolved to favor the formation of dual-topology EmrE dimers over single-topology dimers.
AB - Parallel and antiparallel transmembrane helix–helix interactions support the folding and non-covalent assembly of many integral membrane proteins. While several genetic tools are currently in use to study parallel transmembrane helix–helix interactions, antiparallel associations have been difficult to determine. Here, we present a novel genetic approach, termed BLaTM 2.0, which can be used in combination with the recently presented BLaTM 1.2 to compare the efficiency of antiparallel and parallel transmembrane domain (TMD) interactions in a natural membrane. In a practical application of the BLaTM system, we find that the antiparallel interaction of TMD4, the known dimerization domain of the dual-topology small multidrug transporter EmrE, is sequence-specific and much stronger than the parallel one. This suggests that TMD4 has evolved to favor the formation of dual-topology EmrE dimers over single-topology dimers.
KW - BLaTM
KW - antiparallel interaction, EmrE, multidrug resistance protein
KW - transmembrane domain
UR - http://www.scopus.com/inward/record.url?scp=85018268901&partnerID=8YFLogxK
U2 - 10.1016/j.jmb.2017.04.003
DO - 10.1016/j.jmb.2017.04.003
M3 - Article
C2 - 28432015
AN - SCOPUS:85018268901
SN - 0022-2836
VL - 429
SP - 1630
EP - 1637
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
IS - 11
ER -