Cargando…

Cotranslational protein targeting to the membrane: Nascent-chain transfer in a quaternary complex formed at the translocon

Membrane proteins in bacteria are cotranslationally inserted into the plasma membrane through the SecYEG translocon. Ribosomes exposing the signal-anchor sequence (SAS) of a membrane protein are targeted to the translocon by the signal recognition particle (SRP) pathway. SRP scans translating riboso...

Descripción completa

Detalles Bibliográficos
Autores principales:	Draycheva, Albena, Lee, Sejeong, Wintermeyer, Wolfgang
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2018
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6028451/ https://www.ncbi.nlm.nih.gov/pubmed/29967439 http://dx.doi.org/10.1038/s41598-018-28262-8

Ejemplares similares

Lateral gate dynamics of the bacterial translocon during cotranslational membrane protein insertion
por: Mercier, Evan, et al.
Publicado: (2021)

Electrostatics and Intrinsic Disorder Drive Translocon Binding of the SRP Receptor FtsY
por: Lakomek, Nils‐Alexander, et al.
Publicado: (2016)

Lateral opening of the bacterial translocon on ribosome binding and signal peptide insertion
por: Ge, Yan, et al.
Publicado: (2014)

Ribosome binding induces repositioning of the signal recognition particle receptor on the translocon
por: Kuhn, Patrick, et al.
Publicado: (2015)

Cotranslational Biogenesis of Membrane Proteins in Bacteria
por: Mercier, Evan, et al.
Publicado: (2022)

Ribosome selectivity and nascent chain context in modulating the incorporation of fluorescent non-canonical amino acid into proteins
por: Thommen, Michael, et al.
Publicado: (2022)

Cotranslational Folding Inhibits Translocation from Within the Ribosome–Sec61 Translocon Complex
por: Conti, Brian J., et al.
Publicado: (2014)

Partially inserted nascent chain unzips the lateral gate of the Sec translocon
por: Kater, Lukas, et al.
Publicado: (2019)

An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation
por: Jiang, Ying, et al.
Publicado: (2008)

Defining the Specificity of Cotranslationally Acting Chaperones by Systematic Analysis of mRNAs Associated with Ribosome-Nascent Chain Complexes
por: del Alamo, Marta, et al.
Publicado: (2011)

Charge-driven dynamics of nascent chain movement through the SecYEG translocon
por: Ismail, Nurzian, et al.
Publicado: (2015)

SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo
por: Huber, Damon, et al.
Publicado: (2016)

Gradual compaction of the nascent peptide during cotranslational folding on the ribosome
por: Liutkute, Marija, et al.
Publicado: (2020)

Cotranslational recruitment of ribosomes in protocells recreates a translocon-independent mechanism of proteorhodopsin biogenesis
por: Eaglesfield, Ross, et al.
Publicado: (2021)

Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome
por: Jomaa, Ahmad, et al.
Publicado: (2017)

Glycosylation Can Influence Topogenesis of Membrane Proteins and Reveals Dynamic Reorientation of Nascent Polypeptides within the Translocon
por: Goder, Veit, et al.
Publicado: (1999)

Cotranslational signal independent SRP preloading during membrane targeting
por: Chartron, Justin W., et al.
Publicado: (2016)

Widespread Cotranslational Formation of Protein Complexes
por: Duncan, Caia D. S., et al.
Publicado: (2011)

The ribosome quality control pathway can access nascent polypeptides stalled at the Sec61 translocon
por: von der Malsburg, Karina, et al.
Publicado: (2015)

The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins
por: Shurtleff, Matthew J, et al.
Publicado: (2018)

Kinetic control of nascent protein biogenesis by peptide deformylase
por: Bögeholz, Lena A. K., et al.
Publicado: (2021)

SecA mediates cotranslational targeting and translocation of an inner membrane protein
por: Wang, Shuai, et al.
Publicado: (2017)

Molecular mechanism of cotranslational membrane protein recognition and targeting by SecA
por: Wang, Shuai, et al.
Publicado: (2019)

Nascent chain dynamics and ribosome interactions within folded ribosome–nascent chain complexes observed by NMR spectroscopy
por: Burridge, Charles, et al.
Publicado: (2021)

Fidelity of Cotranslational Protein Targeting to the Endoplasmic Reticulum
por: Hsieh, Hao-Hsuan, et al.
Publicado: (2021)

Residue-by-residue analysis of cotranslational membrane protein integration in vivo
por: Nicolaus, Felix, et al.
Publicado: (2021)

Prefoldin–Nascent Chain Complexes in the Folding of Cytoskeletal Proteins
por: Hansen, William J., et al.
Publicado: (1999)

Dissecting the molecular organization of the translocon-associated protein complex
por: Pfeffer, Stefan, et al.
Publicado: (2017)

Cotranslational Folding of Proteins on the Ribosome
por: Liutkute, Marija, et al.
Publicado: (2020)

Cotranslational assembly of protein complexes in eukaryotes revealed by ribosome profiling
por: Shiber, Ayala, et al.
Publicado: (2018)

Structural inventory of cotranslational protein folding by the eukaryotic RAC complex
por: Kišonaitė, Miglė, et al.
Publicado: (2023)

The expanding role of the ER translocon in membrane protein folding
por: Skach, William R.
Publicado: (2007)

In silico evaluation of the influence of the translocon on partitioning of membrane segments
por: Tessier, Dominique, et al.
Publicado: (2014)

An ER translocon for multi-pass membrane protein biogenesis
por: McGilvray, Philip T, et al.
Publicado: (2020)

NAC covers ribosome-associated nascent chains thereby forming a protective environment for regions of nascent chains just emerging from the peptidyl transferase center
Publicado: (1995)

A ribosome-associated chaperone enables substrate triage in a cotranslational protein targeting complex
por: Hsieh, Hao-Hsuan, et al.
Publicado: (2020)

Large protein complex interfaces have evolved to promote cotranslational assembly
por: Badonyi, Mihaly, et al.
Publicado: (2022)

Cotranslational Protein Folding and Terminus Hydrophobicity
por: Srivastava, Sheenal, et al.
Publicado: (2011)

Evidence of evolutionary selection for cotranslational folding
por: Jacobs, William M., et al.
Publicado: (2017)

Mechanisms of Cotranslational Protein Maturation in Bacteria
por: Koubek, Jiří, et al.
Publicado: (2021)

Cannot write session to /tmp/vufind_sessions/sess_8em9vmu23i9f8og3liehkvjhh7