Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon
Published 2015 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon
Authors
Keywords
-
Journal
JOURNAL OF CELL BIOLOGY
Volume 211, Issue 1, Pages 91-104
Publisher
Rockefeller University Press
Online
2015-10-13
DOI
10.1083/jcb.201502103
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- A new system for naming ribosomal proteins
- (2014) Nenad Ban et al. CURRENT OPINION IN STRUCTURAL BIOLOGY
- Regulation of cargo recognition, commitment, and unloading drives cotranslational protein targeting
- (2014) Ishu Saraogi et al. JOURNAL OF CELL BIOLOGY
- The Sec translocon mediated protein transport in prokaryotes and eukaryotes
- (2014) Kärt Denks et al. MOLECULAR MEMBRANE BIOLOGY
- The actin homologue MreB organizes the bacterial cell membrane
- (2014) Henrik Strahl et al. Nature Communications
- Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion
- (2014) Yan Ge et al. Nature Communications
- Visualization of a polytopic membrane protein during SecY-mediated membrane insertion
- (2014) Lukas Bischoff et al. Nature Communications
- Signal Recognition Particle: An Essential Protein-Targeting Machine
- (2013) David Akopian et al. Annual Review of Biochemistry
- YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein
- (2013) Ilie Sachelaru et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- SecYEG activates GTPases to drive the completion of cotranslational protein targeting
- (2013) David Akopian et al. JOURNAL OF CELL BIOLOGY
- Monitoring the Activity of Single Translocons
- (2013) Intan Taufik et al. JOURNAL OF MOLECULAR BIOLOGY
- The Structural Basis of FtsY Recruitment and GTPase Activation by SRP RNA
- (2013) Felix Voigts-Hoffmann et al. MOLECULAR CELL
- Mitochondrial translation factors ofTrypanosoma brucei:elongation factor-Tu has a unique subdomain that is essential for its function
- (2013) Marina Cristodero et al. MOLECULAR MICROBIOLOGY
- Structure of the SecY channel during initiation of protein translocation
- (2013) Eunyong Park et al. NATURE
- Activities at the Universal Protein Resource (UniProt)
- (2013) NUCLEIC ACIDS RESEARCH
- Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways
- (2013) Renuka Kudva et al. RESEARCH IN MICROBIOLOGY
- Purification and Characterization ofEscherichia coli MreBProtein
- (2012) Pearl Nurse et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Competitive Binding of the SecA ATPase and Ribosomes to the SecYEG Translocon
- (2012) Zht Cheng Wu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Activated GTPase movement on an RNA scaffold drives co-translational protein targeting
- (2012) Kuang Shen et al. NATURE
- Dynamic switch of the signal recognition particle from scanning to targeting
- (2012) Wolf Holtkamp et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Lipids Trigger a Conformational Switch That Regulates Signal Recognition Particle (SRP)-mediated Protein Targeting
- (2011) Goran Stjepanovic et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Mapping of the SecA·SecY and SecA·SecG Interfaces by Site-directedin VivoPhotocross-linking
- (2011) Sanchaita Das et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Andromeda: A Peptide Search Engine Integrated into the MaxQuant Environment
- (2011) Jürgen Cox et al. JOURNAL OF PROTEOME RESEARCH
- Signal sequence–independent SRP-SR complex formation at the membrane suggests an alternative targeting pathway within the SRP cycle
- (2011) David Braig et al. MOLECULAR BIOLOGY OF THE CELL
- Promiscuous targeting of polytopic membrane proteins to SecYEG or YidC by the Escherichia coli signal recognition particle
- (2011) Thomas Welte et al. MOLECULAR BIOLOGY OF THE CELL
- Cryo-EM structure of the ribosome–SecYE complex in the membrane environment
- (2011) Jens Frauenfeld et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The Bacterial SRP Receptor, SecA and the Ribosome Use Overlapping Binding Sites on the SecY Translocon
- (2011) Patrick Kuhn et al. TRAFFIC
- Genetic Evidence for Functional Interaction of theEscherichia coliSignal Recognition Particle Receptor with Acidic Lipidsin Vivo
- (2010) Elinor Erez et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting
- (2010) Vinh Q. Lam et al. JOURNAL OF CELL BIOLOGY
- The action of cardiolipin on the bacterial translocon
- (2010) V. A. M. Gold et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Escherichia coli SRP, Its Protein Subunit Ffh, and the Ffh M Domain Are Able To Selectively Limit Membrane Protein Expression When Overexpressed
- (2010) I. Yosef et al. mBio
- Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor
- (2009) Miryana Mircheva et al. BMC BIOLOGY
- Two Cooperating Helices Constitute the Lipid-binding Domain of the Bacterial SRP Receptor
- (2009) David Braig et al. JOURNAL OF MOLECULAR BIOLOGY
- A Cleavable N-Terminal Membrane Anchor is Involved in Membrane Binding of the Escherichia coli SRP Receptor
- (2008) Benjamin Weiche et al. JOURNAL OF MOLECULAR BIOLOGY
- MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
- (2008) Jürgen Cox et al. NATURE BIOTECHNOLOGY
- Signal sequence–independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnel
- (2008) Thomas Bornemann et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
Create your own webinar
Interested in hosting your own webinar? Check the schedule and propose your idea to the Peeref Content Team.
Create NowAsk a Question. Answer a Question.
Quickly pose questions to the entire community. Debate answers and get clarity on the most important issues facing researchers.
Get Started