Protein Movement Across Membranes
DOI: 10.1007/0-387-30871-7_2
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Preprotein Translocation through the Sec Translocon in Bacteria

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Cited by 2 publications
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“…In bacteria, the Sec complex is composed of three membrane proteins (SecYEG) which conduct polypeptides through or into the cytosolic membrane (for recent reviews, see Rapoport et al , 2004; Veenendaal et al , 2004). Depending on the type of substrate, the Sec complex cooperates with either the ribosome or the ATPase SecA to push the protein by co‐ or post‐translational mechanisms, respectively (Dalbey and Chen, 2004; Luirink and Sinning, 2004; Maillard et al , 2005).…”
Section: Introductionmentioning
confidence: 99%
“…In bacteria, the Sec complex is composed of three membrane proteins (SecYEG) which conduct polypeptides through or into the cytosolic membrane (for recent reviews, see Rapoport et al , 2004; Veenendaal et al , 2004). Depending on the type of substrate, the Sec complex cooperates with either the ribosome or the ATPase SecA to push the protein by co‐ or post‐translational mechanisms, respectively (Dalbey and Chen, 2004; Luirink and Sinning, 2004; Maillard et al , 2005).…”
Section: Introductionmentioning
confidence: 99%
“…The effluent saw an upregulation of secG, sec-C, and secY while the chlorinated effluent saw increases in secF and secE (Tables S4 and S5). The main translocon channel is composed of proteins SecY, SecE and SecG [52]. While secY, secE and secG were not upregulated in both effluents, secG and secY gene were upregulated in the effluent and by the time A. junii transitions to the chlorination chamber, these proteins would already be in abundance.…”
Section: Discussionmentioning
confidence: 93%