Domain organization of long signal peptides of single-pass integral membrane proteins reveals multiple functional capacity.

ABSTRACT: Targeting signals direct proteins to their extra- or intracellular destination such as the plasma membrane or cellular organelles. Here we investigated the structure and function of exceptionally long signal peptides encompassing at least 40 amino acid residues. We discovered a two-domain organization ("NtraC model") in many long signals from vertebrate precursor proteins. Accordingly, long signal peptides may contain an N-terminal domain (N-domain) and a C-terminal domain (C-domain) with different signal or targeting capabilities, separable by a presumably turn-rich transition area (tra). Individual domain functions were probed by cellular targeting experiments with fusion proteins containing parts of the long signal peptide of human membrane protein shrew-1 and secreted alkaline phosphat

SUBMITTER: Hiss JA 

PROVIDER: S-EPMC2447879 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature