Decay of 27-h Ho166

Cline, J.E.; Yates, E. C.; Turk, E.H.

doi:10.1016/0029-5582(62)90040-8

Cited by 24 publications

(11 citation statements)

References 9 publications

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“…Although we could substitute one or two of these residues by alanine, a triple substituted TatB protein was all but inactive. This is of particular interest since it has been proposed that a complex of TatBC forms the initial site of signal peptide binding by the Tat machinery [20], and therefore this highly negative patch is a prime candidate for twin-arginine recognition during the binding event.…”

Section: Discussionmentioning

confidence: 99%

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The Escherichia coli twin‐arginine translocase: conserved residues of TatA and TatB family components involved in protein transport

et al. 2003

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The Escherichia coli Tat system serves to export folded proteins harbouring an N-terminal twin-arginine signal peptide across the cytoplasmic membrane. In this report we have studied the functions of conserved residues within the structurally related TatA and TatB proteins. Our results demonstrate that there are two regions within each protein of high sequence conservation that are critical for e⁄cient Tat translocase function. The ¢rst region is the interdomain hinge between the transmembrane and the amphipathic K K-helices of TatA and TatB proteins. The second region is within the amphipathic helices of TatA and TatB. In particular an invariant phenylalanine residue within TatA proteins is essential for activity, whereas a string of glutamic acid residues on the same face of the amphipathic helix of TatB is important for function.

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Section: Discussionmentioning

confidence: 99%

“…It is highly hydrophobic, with either 4 or 6 transmembrane spans [18,19]. It has been implicated, along with TatB, as the site of recognition of the twinarginine signal peptide [20,17].…”

Section: Introductionmentioning

confidence: 99%

The Escherichia coli twin‐arginine translocase: conserved residues of TatA and TatB family components involved in protein transport

et al. 2003

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“…HiPIP has also been tested and is no exception from this rule [15]. Moreover, it has been shown with the thylakoidal Tat system that the twin-arginine motif is required for a direct interaction with the Tat system components [23]. It must therefore be considered that the twin-arginine motif pattern forms a structure which is speci¢cally recognized by the Tat system.…”

Section: Discussionmentioning

confidence: 99%

Structural studies on a twin‐arginine signal sequence

Kipping

Lilie²,

Lindenstrauß³

et al. 2003

FEBS Letters

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Translocation of folded proteins across biological membranes can be mediated by the so-called 'twin-arginine translocation' (Tat) system. To be translocated, Tat substrates require N-terminal signal sequences which usually contain the eponymous twin-arginine motif. Here we report the ¢rst structural analysis of a twin-arginine signal sequence, the signal sequence of the high potential iron-sulfur protein from Allochromatium vinosum. Nuclear magnetic resonance (NMR) analyses of amide proton resonances did not indicate a signal sequence structure. Accordingly, data from H/D exchange matrix-assisted laser desorption/ionization-time of £ight (MALDI-TOF) mass spectrometry showed that the amide protons of the signal sequence exchange rapidly, indicating the absence of secondary structure in the signal sequence up to L29. We conclude that the conserved twin-arginine motif does not form a structure by itself or as a result of intramolecular interactions. ß

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“…The delta pH pathway uses proton gradient across the thylakoid membrane as sole energy source for protein translocation [32,37], and it involves hcf106, tha4 and tatC gene products [33,38^40]. A TatCĤ cf106 complex has been shown to function as a receptor for the pathway, and subsequent participation of Tha4 leads to translocation [40]. Spontaneous insertion into the thylakoid membrane has also been reported for some proteins [33].…”

Section: Targeting and Insertion Of Nascent D1 Protein Into The Thylamentioning

confidence: 99%

Synthesis, membrane insertion and assembly of the chloroplast‐encoded D1 protein into photosystem II

Zhang

Aro

2002

FEBS Letters

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Rapid light-dependent turnover of the chloroplastencoded D1 protein maintains photosystem II (PS II) functional over a wide range of light intensities. Following initiation of psbA mRNA translation, the elongating D1 is targeted, possibly by chloroplast signal recognition particle 54 (cpSRP54), to the thylakoid cpSecY translocation channel. Transmembrane domains of nascent D1 start interacting with other PS II core proteins already during the translocation process to ensure an efficient assembly of the multiprotein membrane complex. Here we review the progress recently made concerning the synthesis, targeting, membrane insertion and assembly to PS II of the chloroplast-encoded D1 protein and discuss the possible convergence of targeting and translocation of chloroplast-and nuclear-encoded thylakoid proteins. ß

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Decay of 27-h Ho166

Cited by 24 publications

References 9 publications

The Escherichia coli twin‐arginine translocase: conserved residues of TatA and TatB family components involved in protein transport

The Escherichia coli twin‐arginine translocase: conserved residues of TatA and TatB family components involved in protein transport

Structural studies on a twin‐arginine signal sequence

Synthesis, membrane insertion and assembly of the chloroplast‐encoded D1 protein into photosystem II

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