Format

Send to

Choose Destination
See comment in PubMed Commons below
Science. 1987 Feb 13;235(4790):783-7.

Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly.

Abstract

Leader peptidase spans the Escherichia coli plasma membrane with its amino-terminal domain facing the cytoplasm and its carboxyl terminus facing the periplasm. It is made without a cleavable leader sequence. The three apolar domains near the amino terminus of the peptidase are candidates for internal "signal sequences" and they anchor the protein to the lipid bilayer. Oligonucleotide-directed deletion was used to show that only the second domain has an essential function in membrane assembly. While this second apolar domain is crucial for membrane assembly, its continued function when disrupted by arginine suggests that its apolar character per se is not its only important feature.

PMID:
3544218
[PubMed - indexed for MEDLINE]

LinkOut - more resources

Full Text Sources

Other Literature Sources

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire
    Loading ...
    Write to the Help Desk