Influence of hydrophobic matching on association of model transmembrane fragments containing a minimised glycophorin A dimerisation motif.
The principles that govern the folding and packing of membrane proteins are still not completely understood. In the present work, we have revisited the glycophorin A (GpA) dimerisation motif that mediates transmembrane (TM) helix association, one of the best-suited models of membrane protein oligomerisation. By using artificial polyleucine TM segments we have demonstrated in this study that a pattern of only five amino acids (GVxxGVxxT) promotes specific dimerisation. Further, we have used this minimised GpA motif to assess the influence of hydrophobic matching on the TM helix packing process in detergent micelles and found that this factor modulates helix-helix association and/or dissociation between TM fragments.
Orzáez
Mar
M
Departament de Bioquímica i Biologia Molecular, Universitat de València, E-46100 Burjassot, Spain.
Lukovic
Dunja
D
Abad
Concepción
C
Pérez-Payá
Enrique
E
Mingarro
Ismael
I
D020816:Amino Acid Motifs / Q000235:genetics; D000595:Amino Acid Sequence; D000818:Animals; D019281:Dimerization; D006021:Glycophorins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D007930:Leucine / Q000737:chemistry / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D006021:Glycophorins; D008565:Membrane Proteins; D010455:Peptides; D011993:Recombinant Fusion Proteins; C027819:polyleucine; D007930:Leucine