Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. (Q54435413)

29 May 2018

title

Escherichia coli signal recognition particle receptor FtsY contains an essential and autonomous membrane-binding amphipathic helix. (English)

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3

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Gert Bange

5

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Eitan Bibi

6

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author name string

Richard Parlitz

1

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Asa Eitan

2

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Liat Bahari

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Irmgard Sinning

7

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language of work or name

English

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publication date

28 August 2007

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Journal of Biological Chemistry

published in

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volume

282

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issue

44

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page(s)

32176-32184

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Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review).

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Heterodimeric GTPase Core of the SRP Targeting Complex

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Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle

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FtsY, the prokaryotic signal recognition particle receptor homologue, is essential for biogenesis of membrane proteins.

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Dual recognition of the ribosome and the signal recognition particle by the SRP receptor during protein targeting to the endoplasmic reticulum

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Accumulation of endoplasmic membranes and novel membrane-bound ribosome-signal recognition particle receptor complexes in Escherichia coli.

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FtsY, the bacterial signal-recognition particle receptor, interacts functionally and physically with the SecYEG translocon

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Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites

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New prospects in studying the bacterial signal recognition particle pathway.

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Crystal structure of the NG domain from the signal-recognition particle receptor FtsY

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The core Escherichia coli signal recognition particle receptor contains only the N and G domains of FtsY

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SRbeta coordinates signal sequence release from SRP with ribosome binding to the translocon

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The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide

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Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity

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A site-specific, membrane-dependent cleavage event defines the membrane binding domain of FtsY.

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Expression, crystallization and preliminary X-ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli.

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X-ray structure of the T. Aquaticus Ftsy:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases

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X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates

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Amphipathic helix motif: classes and properties

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Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid

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Membrane localization of MinD is mediated by a C-terminal motif that is conserved across eubacteria, archaea, and chloroplasts

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The MinD membrane targeting sequence is a transplantable lipid-binding helix

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Classification and evolution of P-loop GTPases and related ATPases

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Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.

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Role of membrane lipids in bacterial division-site selection

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BIOGENESIS OF INNER MEMBRANE PROTEINS IN ESCHERICHIA COLI

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21 January 2018

Identifiers

DOI

10.1074/JBC.M705430200

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29 May 2018

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29 May 2018