The structural basis of protein targeting and translocation in bacteria

No abstract is available for this paper.

• Publication year

  2001

• Venue

  Nature Structural Biology

• Publication date

  2001-06-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1038/88549PMID 11373615
• 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.

• Oxa1p acts as a general membrane insertion machinery for proteins encoded by mitochondrial DNA

  2001cited by this paper
• Discrimination between SRP‐ and SecA/SecB‐dependent substrates involves selective recognition of nascent chains by SRP and trigger factor

  2000cited by this paper
• SecYEG assembles into a tetramer to form the active protein translocation channel

  2000cited by this paper
• Escherichia coli translocase: the unravelling of a molecular machine

  2000cited by this paper
• Crystal structure of the bacterial protein export chaperone SecB

  2000cited by this paper
• SRP‐dependent co‐translational targeting and SecA‐dependent translocation analyzed as individual steps in the export of a bacterial protein

  2000cited by this paper
• YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

  2000cited by this paper
• YidC mediates membrane protein insertion in bacteria

  2000cited by this paper
• Two Independent Mechanisms Down-regulate the Intrinsic SecA ATPase Activity*

  2000cited by this paper
• New prospects in studying the bacterial signal recognition particle pathway

  2000cited by this paper
• Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA

  2000cited by this paper
• Crystal structure of the ribonucleoprotein core of the signal recognition particle.

  2000cited by this paper
• The structure of ribosome-channel complexes engaged in protein translocation.

  2000cited by this paper
• Evaluating the oligomeric state of SecYEG in preprotein translocase

  2000cited by this paper
• Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP

  1999cited by this paper
• A molecular switch in SecA protein couples ATP hydrolysis to protein translocation

  1999cited by this paper
• Cysteine-directed cross-linking demonstrates that helix 3 of SecE is close to helix 2 of SecY and helix 3 of a neighboring SecE.

  1999cited by this paper
• Protein Targeting to the Bacterial Cytoplasmic Membrane

  1999cited by this paper
• The translocon: a dynamic gateway at the ER membrane.

  1999cited by this paper
• Validation of the Nordic Flow Cytometry Standard for CD34+ Cell Enumeration in Blood and Autografts: Report from the Third Workshop

  1999cited by this paper
• The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex.

  1999cited by this paper
• Substrate Specificity of the SecB Chaperone*

  1999cited by this paper
• Mutational Alterations in the Homotetrameric Chaperone SecB That Implicate the Structure as Dimer of Dimers*

  1999cited by this paper
• Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA

  1998cited by this paper
• Calorimetric analyses of the interaction between SecB and its ligands

  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 signal sequence binding subunit of the signal recognition particle.

  1998cited by this paper
• Escherichia coli SecA shape and dimensions

  1998cited by this paper
• Translocase-bound SecA is largely shielded from the phospholipid acyl chains.

  1998cited by this paper
• The Escherichia coli SRP and SecB targeting pathways converge at the translocon

  1998cited by this paper
• The catalytic cycle of the Escherichia coli SecA ATPase comprises two distinct preprotein translocation events

  1997cited by this paper
• The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane.

  1997cited by this paper
• The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling

  1997cited by this paper
• Structure of the conserved GTPase domain of the signal recognition particle

  1997cited by this paper
• Topology of the Integral Membrane Form of Escherichia coli SecA Protein Reveals Multiple Periplasmically Exposed Regions and Modulation by ATP Binding*

  1997cited by this paper
• The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain.

  1997cited by this paper
• Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex.

  1997cited by this paper
• Domain interactions in E. coli SRP: stabilization of M domain by RNA is required for effective signal sequence modulation of NG domain.

  1997cited by this paper
• Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation.

  1997cited by this paper
• The molecular chaperone SecB is released from the carboxy‐terminus of SecA during initiation of precursor protein translocation

  1997cited by this paper
• Crystal structure of the NG domain from the signal-recognition particle receptor FtsY

  1997cited by this paper
• Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation.

  1996cited by this paper
• Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases

  1995cited by this paper
• Evolutionary conservation of components of the protein translocation complex

  1994cited by this paper
• Determination of the binding frame within a physiological ligand for the chaperone SecB

  1994cited by this paper
• SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

  1994cited by this paper
• Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.

  1994cited by this paper
• Highly selective binding of nascent polypeptides by an Escherichia coli chaperone protein in vivo

  1993cited by this paper
• The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids.

  1993cited by this paper
• Membrane vesicles containing overproduced SecY and SecE exhibit high translocation ATPase activity and countermovement of protons in a SecA- and presecretory protein-dependent manner.

  1993cited by this paper
• ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

  1991cited by this paper
• A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB.

  1991cited by this paper
• The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane.

  1990cited by this paper
• Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization.

  1990cited by this paper
• Modulation of folding pathways of exported proteins by the leader sequence.

  1988cited by this paper

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