E Park, TA Rapoport - Annual review of biophysics, 2012 - annualreviews.org
The Sec61 or SecY channel, a universally conserved protein-conducting channel, translocates proteins across and integrates proteins into the eukaryotic endoplasmic …
About 25% to 30% of the bacterial proteins function in the cell envelope or outside of the cell. These proteins are synthesized in the cytosol, and the vast majority is recognized as a …
Recognition of signal sequences by cognate receptors controls the entry of virtually all proteins to export pathways. Despite its importance, this process remains poorly understood …
DJF Du Plessis, N Nouwen, AJM Driessen - Biochimica et Biophysica Acta …, 2011 - Elsevier
The vast majority of proteins trafficking across or into the bacterial cytoplasmic membrane occur via the translocon. The translocon consists of the SecYEG complex that forms an …
K Denks, A Vogt, I Sachelaru, NA Petriman… - Molecular membrane …, 2014 - Taylor & Francis
Protein transport via the Sec translocon represents an evolutionary conserved mechanism for delivering cytosolically-synthesized proteins to extra-cytosolic compartments. The Sec …
E Papanikou, S Karamanou, A Economou - Nature Reviews …, 2007 - nature.com
All cells must traffic proteins across their membranes. This essential process is responsible for the biogenesis of membranes and cell walls, motility and nutrient scavenging and uptake …
Over 30% of proteins are secreted across or integrated into membranes. Their newly synthesized forms contain either cleavable signal sequences or non-cleavable membrane …
JA Lycklama a Nijeholt… - … Transactions of the …, 2012 - royalsocietypublishing.org
Most bacterial secretory proteins pass across the cytoplasmic membrane via the translocase, which consists of a protein-conducting channel SecYEG and an ATP …
JM Crane, LL Randall - EcoSal Plus, 2017 - Am Soc Microbiol
In Escherichia coli, proteins found in the periplasm or the outer membrane are exported from the cytoplasm by the general secretory, Sec, system before they acquire stably folded …