Synthetic signal sequences that enable efficient secretory protein production in the yeast Kluyveromyces marxianus.

ABSTRACT:

Background

Targeting of cellular proteins to the extracellular environment is directed by a secretory signal sequence located at the N-terminus of a secretory protein. These signal sequences usually contain an N-terminal basic amino acid followed by a stretch containing hydrophobic residues, although no consensus signal sequence has been identified. In this study, simple modeling of signal sequences was attempted using Gaussia princeps secretory luciferase (GLuc) in the yeast Kluyveromyces marxianus, which allowed comprehensive recombinant gene construction to substitute synthetic signal sequences.

Results

Mutational analysis of the GLuc signal sequence revealed that the GLuc hydrophobic peptide length was lower limit for effective secretion and that the N-terminal basic res

SUBMITTER: Yarimizu T 

PROVIDER: S-EPMC4347551 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature