SecYEG activates GTPases to drive the completion of cotranslational protein targeting

SecYEG drives conformational changes in the cotranslational targeting complex to activate it for GTP hydrolysis and the handover of the translating ribosome.

• Publication year

  2013

• Venue

  Journal of Cell Biology

• Publication date

  2013-02-18

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1083/jcb.201208045PMID 23401005PMCID 3575545
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• University of Groningen Reconstitution of Purified Bacterial Preprotein Translocase in Liposomes Does

  2017cited by this paper
• Two copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase

  2012cited by this paper
• Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle

  2011cited by this paper
• The Sec translocase.

  2011cited by this paper
• Cryo–EM structure of the ribosome–SecYE complex in the membrane environment

  2011cited by this paper
• The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon

  2011cited by this paper
• Site-specific fluorescent labeling of nascent proteins on the translating ribosome.

  2011cited by this paper
• A single copy of SecYEG is sufficient for preprotein translocation

  2011influential reference
• Preserving the membrane barrier for small molecules during bacterial protein translocation

  2011cited by this paper
• The Oligomeric State and Arrangement of the Active Bacterial Translocon*

  2010cited by this paper
• Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting

  2010cited by this paper
• The action of cardiolipin on the bacterial translocon

  2010cited by this paper
• Genetic Evidence for Functional Interaction of the Escherichia coli Signal Recognition Particle Receptor with Acidic Lipids in Vivo*

  2010cited by this paper
• Reconstitution of the SecY translocon in nanodiscs.

  2010cited by this paper
• Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting

  2010cited by this paper
• Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.

  2009cited by this paper
• The Lateral Gate of SecYEG Opens during Protein Translocation*

  2009cited by this paper
• Delivering proteins for export from the cytosol

  2009cited by this paper
• Multiple conformational switches in a GTPase complex control co-translational protein targeting

  2009cited by this paper
• Structure of Monomeric Yeast and Mammalian Sec61 Complexes Interacting with the Translating Ribosome

  2009cited by this paper
• Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.

  2008cited by this paper
• Protein translocation across the bacterial cytoplasmic membrane.

  2008cited by this paper
• Preprotein‐controlled catalysis in the helicase motor of SecA

  2007cited by this paper
• Escherichia coli Signal Recognition Particle Receptor FtsY Contains an Essential and Autonomous Membrane-binding Amphipathic Helix*

  2007cited by this paper
• Ribosome binding of a single copy of the SecY complex: implications for protein translocation.

  2007cited by this paper
• Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA

  2007cited by this paper
• Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation

  2007cited by this paper
• Generation of ribosome nascent chain complexes for structural and functional studies.

  2007cited by this paper
• Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites

  2006cited by this paper
• Signal Recognition Particle Receptor Exposes the Ribosomal Translocon Binding Site

  2006cited by this paper
• Helical distribution of the bacterial chemoreceptor via colocalization with the Sec protein translocation machinery

  2006cited by this paper
• FtsY, the bacterial signal‐recognition particle receptor, interacts functionally and physically with the SecYEG translocon

  2005cited by this paper
• Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY

  2005cited by this paper
• Subcellular sites for bacterial protein export

  2004cited by this paper
• X-ray structure of a protein-conducting channel

  2004cited by this paper
• Substrate twinning activates the signal recognition particle and its receptor

  2004cited by this paper
• Mechanism of Association and Reciprocal Activation of Two GTPases

  2004cited by this paper
• The Core Escherichia coli Signal Recognition Particle Receptor Contains Only the N and G Domains of FtsY

  2004cited by this paper
• Structural determinants of SecB recognition by SecA in bacterial protein translocation

  2003cited by this paper
• Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase

  2003cited by this paper
• Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene‐labelled phospholipids

  2003cited by this paper
• SRβ coordinates signal sequence release from SRP with ribosome binding to the translocon

  2001cited by this paper
• Role of SRP RNA in the GTPase cycles of Ffh and FtsY.

  2001cited by this paper
• Anionic phospholipids are involved in membrane association of FtsY and stimulate its GTPase activity

  2000cited by this paper
• Role of Sec61α in the Regulated Transfer of the Ribosome–Nascent Chain Complex from the Signal Recognition Particle to the Translocation Channel

  2000cited by this paper
• Visualization of membrane domains in Escherichia coli

  1999cited by this paper
• Signal Sequence Recognition in Cotranslational Translocation by Protein Components of the Endoplasmic Reticulum Membrane

  1998cited by this paper
• Interaction between SecA and SecYEG in micellar solution and formation of the membrane-inserted state.

  1998cited by this paper
• Crystal structure of the NG domain from the signal-recognition particle receptor FtsY

  1997cited by this paper
• Expression, crystallization and preliminary X‐ray diffraction study of FtsY, the docking protein of the signal recognition particle of E. coli

  1997cited by this paper
• A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane.

  1995cited by this paper
• Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.

  1994cited by this paper
• Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane.

  1993cited by this paper
• The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

  1990cited by this paper
• An E. coli ribonucleoprotein containing 4.5S RNA resembles mammalian signal recognition particle.

  1990influential reference
• The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.

  1990cited by this paper
• SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

  1989cited by this paper
• COLORIMETRIC METHOD FOR DETER-MINATION OF SUGAR AND RELATED SUBSTANCE

  1956influential reference
• A – E

  1955cited by this paper

• Mechanistic insights into protein biogenesis and maturation on the ribosome.

  2025cites this paper
• Assembly of Macromolecular Complexes in the Whole-Cell Model of a Minimal Cell

  2025cites this paper
• Secretion-Catalyzed Assembly of Protein Biomaterials on a Bacterial Membrane Surface.

  2023cites this paper
• Ribosome-membrane crosstalk: Co-translational targeting pathways of proteins across membranes in prokaryotes and eukaryotes.

  2022cites this paper
• Co-translational membrane targeting and holo-translocon docking of ribosomes translating the SRP receptor.

  2022cites this paper
• Anti-Osteoclast Effect of Exportin-1 Inhibitor Eltanexor on Osteoporosis Depends on Nuclear Accumulation of IκBα–NF-κB p65 Complex

  2022cites this paper
• Archaeal SRP RNA and SRP19 facilitate the assembly of SRP54-FtsY targeting complex.

  2021cites this paper
• The Dynamic SecYEG Translocon

  2021cites this paper
• Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum

  2021cites this paper
• To the Surface and Back: Exo- and Endocytic Pathways in Trypanosoma brucei

  2021cites this paper
• Molecular Mimicry of SecA and Signal Recognition Particle Binding to the Bacterial Ribosome

  2019cites this paper
• Molecular mechanism of cotranslational membrane protein recognition and targeting by SecA

  2019cites this paper
• Structure, dynamics and interactions of large SRP variants

  2019cites this paper
• The SRP signal sequence of KdpD

  2019cites this paper
• Non-competitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in E. coli

  2019cites this paper
• Guiding Tail-anchored Membrane Proteins to the ER In a Chaperone Cascade

  2019cites this paper
• Guiding tail-anchored membrane proteins to the endoplasmic reticulum in a chaperone cascade

  2019cites this paper
• Protein Transport Across the Bacterial Plasma Membrane by the Sec Pathway

  2019cites this paper
• Noncompetitive binding of PpiD and YidC to the SecYEG translocon expands the global view on the SecYEG interactome in Escherichia coli

  2019cites this paper
• Co‐translational protein targeting in bacteria

  2018cites this paper
• Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon

  2018cites this paper
• Biophysical Analysis of Sec-Mediated Protein Translocation in Nanodiscs

  2018cites this paper
• Thylakoid Protein Targeting/Insertion by a Signal Recognition Particle in Chloroplasts

  2017influential citation
• Spatial control of mRNA stability in yeast

  2017cites this paper
• DOMAIN 4 SYNTHESIS AND PROCESSING OF MACROMOLECULES Targeting and Insertion of Membrane Proteins

  2017cites this paper
• Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome

  2017cites this paper
• From bacteria to chloroplasts: evolution of the chloroplast SRP system

  2017cites this paper
• Two-step membrane binding by the bacterial SRP receptor enable efficient and accurate Co-translational protein targeting

  2017influential citation
• Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon

  2016cites this paper
• Analyzing Single-Molecule Protein Transportation Experiments via Hierarchical Hidden Markov Models

  2016cites this paper
• ATPase and GTPase Tangos Drive Intracellular Protein Transport.

  2016cites this paper
• Functional and structural studies of a C-terminally extended YidC

  2016influential citation
• The bacterial SRP receptor, FtsY, is activated on binding to the translocon

  2016cites this paper
• Fidelity of Co-translational Protein Targeting by the Signal Recognition Particle

  2015cites this paper
• Dynamics of co-translational protein targeting.

  2015cites this paper
• Mammalian SRP receptor switches the Sec61 translocase from Sec62 to SRP-dependent translocation

  2015cites this paper
• Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon

  2015cites this paper
• Ribosome–SRP–FtsY cotranslational targeting complex in the closed state

  2015cites this paper
• Multiply labeling proteins for studies of folding and stability.

  2015cites this paper
• Biophysical characterisation of LcrH, a class II chaperone of the type III secretion system

  2015cites this paper
• Role of the PduL enzyme in the function of primitive bacterial organelles found in Salmonella

  2014cites this paper
• Phospholipids and a Protein-Conducting Channel Regulate Cotranslational Protein Targeting

  2014cites this paper
• YlxM Is a Newly Identified Accessory Protein That Influences the Function of Signal Recognition Particle Pathway Components in Streptococcus mutans

  2014cites this paper
• Components in Streptococcus mutans Signal Recognition Particle Pathway Protein That Influences the Function of YlxM Is a Newly Identified Accessory

  2014cites this paper
• Interaction of the SecYEG translocon with SRP receptor and the ribosome.

  2014cites this paper
• Dynamic Interaction of the Sec Translocon with the Chaperone PpiD*

  2014cites this paper
• Multi-state targeting machinery govern the fidelity and efficiency of protein localization.

  2014cites this paper
• Secretome of obligate intracellular Rickettsia.

  2014cites this paper
• Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting

  2014cites this paper
• Fidelity of cotranslational protein targeting by the signal recognition particle.

  2014cites this paper
• Co-translational protein targeting to the bacterial membrane.

  2014influential citation
• The Sec translocon mediated protein transport in prokaryotes and eukaryotes

  2014cites this paper
• Molecular Mechanism of GTPase Activation at the Signal Recognition Particle (SRP) RNA Distal End*

  2013cites this paper
• Particle ( SRP ) RNA Distal End Activation at the Signal Recognition Molecular Mechanism of GTPase RNA

  2013cites this paper
• The structural basis of FtsY recruitment and GTPase activation by SRP RNA.

  2013cites this paper
• Precise timing of ATPase activation drives targeting of tail-anchored proteins

  2013cites this paper
• SecYEG gets grabby with new proteins

  2013cites this paper
• Jcb: Article

  year unknowncites this paper