Results 71 to 80 of about 3,879 (192)

SecA – a new twist in the tail [PDF]

open access: yes, 2016
A paper published in this issue of the Journal of Bacteriology (D. Huber, M. Jamshad, R. Hanmer, D. Schibich, K. Döring, I. Marcomini, G. Kramer, and B. Bukau, J Bacteriol 199:e0622-16, 2017, https://doi.org/10.1128/JB.00622-16) provides us with a timely
Collinson, Ian
core   +2 more sources

Decoding Microbial Plastic Colonisation: Multi‐Omic Insights Into the Fast‐Evolving Dynamics of Early‐Stage Biofilms

open access: yesPROTEOMICS, Volume 25, Issue 7, April 2025.
ABSTRACT Marine plastispheres represent dynamic microhabitats where microorganisms colonise plastic debris and interact. Metaproteomics has provided novel insights into the metabolic processes within these communities; however, the early metabolic interactions driving the plastisphere formation remain unclear.
Charlotte E. Lee   +3 more
wiley   +1 more source

A single copy of SecYEG is sufficient for preprotein translocation [PDF]

open access: yesThe EMBO Journal, 2011
The heterotrimeric SecYEG complex comprises a protein-conducting channel in the bacterial cytoplasmic membrane. SecYEG functions together with the motor protein SecA in preprotein translocation. Here, we have addressed the functional oligomeric state of SecYEG when actively engaged in preprotein translocation.
Kedrov, Alexej   +3 more
openaire   +3 more sources

Bacterial Signal Peptides- Navigating the Journey of Proteins

open access: yesFrontiers in Physiology, 2022
In 1971, Blobel proposed the first statement of the Signal Hypothesis which suggested that proteins have amino-terminal sequences that dictate their export and localization in the cell.
Sharbani Kaushik   +2 more
doaj   +1 more source

Molecular Mechanism of GTPase Activation at the Signal Recognition Particle (SRP) RNA Distal End [PDF]

open access: yes, 2013
The signal recognition particle (SRP) RNA is a universally conserved and essential component of the SRP that mediates the co-translational targeting of proteins to the correct cellular membrane.
Feigon, Juli   +5 more
core   +1 more source

Permeabilisation of the Outer Membrane of Escherichia coli for Enhanced Transport of Complex Molecules

open access: yesMicrobial Biotechnology, Volume 18, Issue 3, March 2025.
Access to synthetic compounds in the bacterial cytoplasm is hindered by the selective cell envelope, particularly in Gram‐negative bacteria like Escherichia coli. This study systematically compares three outer membrane proteins (OMPs) and their engineered variants, highlighting the potential of OMP engineering for the permeabilisation of the outer ...
Ivan Casas‐Rodrigo   +6 more
wiley   +1 more source

Distinct Requirements for Tail-Anchored Membrane Protein Biogenesis in Escherichia coli

open access: yesmBio, 2019
Tail-anchored membrane proteins (TAMPs) are a distinct subset of inner membrane proteins (IMPs) characterized by a single C-terminal transmembrane domain (TMD) that is responsible for both targeting and anchoring.
Markus Peschke   +7 more
doaj   +1 more source

Taming membranes: functional immobilization of biological membranes in hydrogels. [PDF]

open access: yesPLoS ONE, 2011
Single molecule studies on membrane proteins embedded in their native environment are hampered by the intrinsic difficulty of immobilizing elastic and sensitive biological membranes without interfering with protein activity.
Ilja Kusters   +5 more
doaj   +1 more source

Fidelity of Cotranslational Protein Targeting by the Signal Recognition Particle [PDF]

open access: yes, 2014
Accurate folding, assembly, localization, and maturation of newly synthesized proteins are essential to all cells and require high fidelity in the protein biogenesis machineries that mediate these processes.
Shan, Shu-ou, Zhang, Xin
core   +1 more source

Multiple Chaperone DnaK–FliC Flagellin Interactions are Required for Pseudomonas aeruginosa Flagellum Assembly and Indicate a New Function for DnaK

open access: yesMicrobial Biotechnology, Volume 18, Issue 2, February 2025.
The dogma on the heat shock DnaK chaperone establishes its fundamental cytosolic role in folding and unfolding intracellular proteins. This study reveals its tight association with the flagellin, its secretion, likely through the flagellum apparatus, its insertion into a growing flagellum filament and a novel extracellular ATP‐independent chaperone ...
Gabriella Molinari   +17 more
wiley   +1 more source

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