Fine structure of a membrane anchor domain

Nicholas G. Davis, Jef D. Boeke, Peter Model

Research output: Contribution to journalArticle

Abstract

We describe a detailed deletion analysis of the anchoring domain of a model membrane protein. Removal of the 23 contiguous uncharged amino acids from the carboxy terminus of the bacteriophage f1 gene III protein (pIII) converts it from an integral membrane protein to a secreted periplasmic form. Deletions that remove six or fewer residues of the hydrophobic core result in no diminution of the protein's capacity to anchor in the membrane. Longer deletions into this hydrophobic domain gradually destabilize the protein-membrane association. pIII derivatives with over half of the hydrophobic core deleted retain substantial residual anchor function. The basic residues, arginine and lysine, which provide a carboxy-terminal boundary for this domain, can be deleted without loss of anchoring capacity.

Original languageEnglish (US)
Pages (from-to)111-121
Number of pages11
JournalJournal of Molecular Biology
Volume181
Issue number1
DOIs
StatePublished - Jan 5 1985
Externally publishedYes

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Membrane Proteins
Membranes
Bacteriophages
Lysine
Arginine
Proteins
Amino Acids

ASJC Scopus subject areas

  • Virology

Cite this

Fine structure of a membrane anchor domain. / Davis, Nicholas G.; Boeke, Jef D.; Model, Peter.

In: Journal of Molecular Biology, Vol. 181, No. 1, 05.01.1985, p. 111-121.

Research output: Contribution to journalArticle

Davis, Nicholas G. ; Boeke, Jef D. ; Model, Peter. / Fine structure of a membrane anchor domain. In: Journal of Molecular Biology. 1985 ; Vol. 181, No. 1. pp. 111-121.
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