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PMID: 3025188 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The signal sequence suffices to direct export of outer membrane protein OmpA of Escherichia coli K-12.

Journal of bacteriology ·Vol. 169 ·No. 1 ·1987-01-00 ·Pages 66-71

Freudl R, Schwarz H, Degen M, Henning U

Abstract

We studied whether information required for export is present within the mature form of the Escherichia coli 325-residue outer membrane protein OmpA. We had previously analyzed overlapping internal deletions in the ompA gene, and the results allowed us to conclude that if such information exists it must be present repeatedly within the membrane part of the protein encompassing amino acid residues 1 to 177 (R. Freudl, H. Schwarz, M. Klose, N. R. Movva, and U. Henning, EMBO J. 4:3593-3598, 1985). A deletion which removed the codons for amino acid residues 1 to 229 of the OmpA protein was constructed. In this construct the signal sequence was fused to the periplasmic part of the protein. The resulting protein, designated Pro-OmpA delta 1-229, was processed, and the mature 95-residue protein accumulated in the periplasm. Hence, information required for export does not exist within the OmpA protein.

MeSH Terms
Amino Acid Sequence Biological Transport, Active Chromosome Deletion DNA Restriction Enzymes/metabolism Escherichia coli/analysis Gene Expression Regulation Microscopy, Electron Organophosphorus Compounds/metabolism Trypsin/metabolism
Chemicals
Organophosphorus Compounds octamethyl pyrophosphoramide DNA Restriction Enzymes Trypsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Freudl R
Schwarz H
Degen M
Henning U
References (36)
36 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/jb.169.1.66-71.1987
Published
1987-01-00
Pages
66-71
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC211734
Subset
IM
External Links
PubMed source DOI: 10.1128/jb.169.1.66-71.1987 PMC Full Text View journal details
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