Efficient integration of transmembrane domains depends on the folding properties of the upstream sequences.

ABSTRACT: The topology of most membrane proteins is defined by the successive integration of α-helical transmembrane domains at the Sec61 translocon. The translocon provides a pore for the transfer of polypeptide segments across the membrane while giving them lateral access to the lipid. For each polypeptide segment of ∼20 residues, the combined hydrophobicities of its constituent amino acids were previously shown to define the extent of membrane integration. Here, we discovered that different sequences preceding a potential transmembrane domain substantially affect its hydrophobicity requirement for integration. Rapidly folding domains, sequences that are intrinsically disordered or very short or capable of binding chaperones with high affinity, allow for efficient transmembrane integration with lo

SUBMITTER: Janoschke M 

PROVIDER: S-EPMC8379923 | biostudies-literature | 2021 Aug

REPOSITORIES: biostudies-literature