Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work? (Q63359824)

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21 December 2019

title

Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work? (English)

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21 December 2019

3

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21 December 2019

author name string

Kakoli Mitra

series ordinal

1

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21 December 2019

Joachim Frank

series ordinal

2

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21 December 2019

publication date

1 November 2006

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Nature Structural & Molecular Biology

21 December 2019

published in

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21 December 2019

volume

13

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21 December 2019

issue

11

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21 December 2019

page(s)

957-964

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https://scigraph.springernature.com/pub.10.1038/nsmb1166

21 December 2019

exact match

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cites work

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The oligomeric distribution of SecYEG is altered by SecA and translocation ligands

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The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain

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Homology of 54K protein of signal-recognition particle, docking protein and two E. coli proteins with putative GTP-binding domains

31 March 2020

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Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum

31 March 2020

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Role of Sec61alpha in the regulated transfer of the ribosome-nascent chain complex from the signal recognition particle to the translocation channel

31 March 2020

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The signal recognition particle

31 March 2020

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A GTP-binding protein of Mycoplasma hominis: a small sized homolog to the signal recognition particle receptor FtsY.

31 March 2020

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Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum

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Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting

31 March 2020

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The beta-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the beta-subunit of the signal recognition particle receptor

31 March 2020

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Structure of the signal recognition particle interacting with the elongation-arrested ribosome.

31 March 2020

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Mechanism of association and reciprocal activation of two GTPases

31 March 2020

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

31 March 2020

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Structural basis for the function of the beta subunit of the eukaryotic signal recognition particle receptor

31 March 2020

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Evidence for a novel GTPase priming step in the SRP protein targeting pathway

31 March 2020

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Heterodimeric GTPase Core of the SRP Targeting Complex

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Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases

31 March 2020

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Distinct modes of signal recognition particle interaction with the ribosome

31 March 2020

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The ribosome regulates the GTPase of the beta-subunit of the signal recognition particle receptor

31 March 2020

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

31 March 2020

1 reference

Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum

31 March 2020

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Elongation arrest by SecM via a cascade of ribosomal RNA rearrangements

31 March 2020

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Signal sequences initiate the pathway of maturation in the endoplasmic reticulum lumen.

31 March 2020

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YidC and SecY mediate membrane insertion of a Type I transmembrane domain.

31 March 2020

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Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

31 March 2020

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Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

31 March 2020

1 reference

Binding of SecA to the SecYEG complex accelerates the rate of nucleotide exchange on SecA.

31 March 2020

1 reference

ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

31 March 2020

1 reference

The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

31 March 2020

1 reference

Crystal structure of the bacterial protein export chaperone secB

31 March 2020

1 reference

Substrate specificity of the SecB chaperone

31 March 2020

1 reference

The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.

31 March 2020

1 reference

Structural determinants of SecB recognition by SecA in bacterial protein translocation

31 March 2020

1 reference

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

31 March 2020

1 reference

Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.

31 March 2020

1 reference

Global co-ordination of protein translocation by the SecA IRA1 switch

31 March 2020

1 reference

Identification of Two Interaction Sites in SecY that Are Important for the Functional Interaction with SecA

31 March 2020

1 reference

The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules

31 March 2020

1 reference

Covalently dimerized SecA is functional in protein translocation

31 March 2020

1 reference

Dimeric SecA is essential for protein translocation

31 March 2020

1 reference

Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy

31 March 2020

1 reference

Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.

31 March 2020

1 reference

31 March 2020

Identifiers

DOI

10.1038/NSMB1166

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:17082791%20AND%20SRC:MED&resulttype=core&format=json

Dimensions Publication ID

21 December 2019

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