A simple test for a conductor

Yamana, Shukichi; Yamana, Hikaru; Yamana, Hideaki

doi:10.1021/ed046p354

Cited by 2 publications

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“…The introduction of positively charged residues after the leader peptide of the alkaline phosphatase (Li et al, 1988), lipoprotein (Yamana and Mizushima, 1988) and the M13 precursor protein (R. Dalbey and A.Kuhn, in preparation) inhibits membrane insertion. Strikingly, these studies as well as our studies shown here indicate that the dipolar structure of leader or signal peptides, with a positive net charge difference between the amino-and carboxy-terminal segments (Von Heijne, 1986), is important for export.…”

Section: Discussionmentioning

confidence: 99%

Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.

Laws

Dalbey

1989

The EMBO Journal

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Leader peptidase, an integral transmembrane protein of Escherichia coli, requires two apolar topogenic elements for its membrane assembly: a 'hydrophobic helper' and an internal signal. The highly basic cytoplasmic region between these domains is a translocation poison sequence, which we have shown blocks the function of a preceding signal sequence. We have used oligonucleotide-directed mutagenesis to remove positively charged residues within this polar domain to determine if it is the basic character in this region that has the negative effect on translocation. Our results show that mutations that remove two or more of the positively charged residues within the polar region no longer block membrane assembly of leader peptidase. In addition, when the translocation poison domain (residues 30-52) is replaced with six lysine residues, the preceding apolar domain cannot function as an export signal, whereas it can with six glutamic acids. Thus, positively charged residues within membrane proteins may have a major role in determining the function of hydrophobic domains in membrane assembly.

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Section: Discussionmentioning

confidence: 99%

Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.

Laws

Dalbey

1989

The EMBO Journal

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“…The construction of paper models of useful molecular structures had been discussed recently in several articles (1)(2)(3)(4)(5) published in the Journal. We now report a convergent approach to the construction of the model of trigonal bipyramid, cube, and triakis octahedron, all from one common basic folding unit.…”

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confidence: 99%

A convergent approach to models of trigonal bipyramid, cube, and triakis octahedron

Lam‐Leung

Lee²,

Tsang

et al. 1991

J. Chem. Educ.

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A simple test for a conductor

Abstract: An ordinary fluorescent lamp can be used to test whether a substance is a conductor or not.

Cited by 2 publications

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Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.

Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal.

A convergent approach to models of trigonal bipyramid, cube, and triakis octahedron

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