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Determinants of membrane protein topology.

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Boyd, D, Manoil, C, Beckwith, J·1987·Proceedings of the National Academy of Sciences

Abstract

The topology of the integral membrane protein MalF, which is required for maltose transport in Escherichia coli, has been analyzed using fusions of alkaline phosphatase (EC 3.1.3.1). The properties of such fusion strains support a MalF structure previously proposed on theoretical grounds. Several transmembrane segments within MalF can act as signal sequences in exporting alkaline phosphatase. Other transmembrane sequences, in conjunction with cytoplasmic domains, can stably anchor alkaline phosphatase in the cytoplasm. Our results suggest that features of the amino acid sequence (possibly the positively charged amino acids) of the cytoplasmic domains of membrane proteins are important in anchoring these domains in the cytoplasm. These studies in conjunction with our earlier results show that alkaline phosphatase fusions to membrane proteins can be an important aid in analyzing membrane topology and its determinants.

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Metadata

Authors
Boyd, D., Manoil, C., & Beckwith, J.
Venue
Proceedings of the National Academy of Sciences
Published
1987-12
Volume
84
Issue
23
Pages
8525-8529
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2029766804
Cited by
295
References
0
FWCI
11.01
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Determinants of membrane protein topology. https://app.cochat.ai/papers/10.1073/pnas.84.23.8525
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Boyd, D., Manoil, C., & Beckwith, J. (1987). Determinants of membrane protein topology. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.84.23.8525

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