Results 191 to 199 of about 34,551 (199)

Reconstitution of functionally efficient SecA-dependent protein-conducting channels: Transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels

Biochemical and Biophysical Research Communications, 2013
Previous work showed that SecA alone can promote protein translocation and ion-channel activity in liposomes, and that SecYEG increases efficiency as well as signal peptide specificity. We now report that SecDF·YajC further increases translocation and ion-channel activity. These activities of reconstituted SecA-SecYEG-SecDF·YajC-liposome are almost the
Ying-hsin, Hsieh, Hao, Zhang, Hongyun, Wang, Hsiuchin, Yang, Chun, Jiang, Sen-fang, Sui, Phang C, Tai   +6 more
openaire   +2 more sources

Control of SecA and SecM translation by protein secretion

Current Opinion in Microbiology, 2004
SecA, the protein translocation ATPase of E. coli is subject to secretion-defect-response control. SecM (secretion monitor) encoded by the 5' region of the secM-secA mRNA is involved in this regulation. SecM translation is subject to transient elongation arrest at Pro166, which is prolonged when export of the nascent SecM is blocked.
Hitoshi, Nakatogawa, Akiko, Murakami, Koreaki, Ito   +2 more
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A molecular switch in SecA protein couples ATP hydrolysis to protein translocation

Molecular Microbiology, 1999
SecA, the dimeric ATPase subunit of bacterial protein translocase, catalyses translocation during ATP‐driven membrane cycling at SecYEG. We now show that the SecA protomer comprises two structural modules: the ATPase N‐domain, containing the nucleotide binding sites NBD1 and NBD2, and the regulatory C‐domain.
S, Karamanou, E, Vrontou, G, Sianidis, C, Baud, T, Roos, A, Kuhn, A S, Politou, A, Economou   +7 more
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Stability and Solvent Accessibility of SecA Protein of Escherichia coli

Journal of Biochemistry, 1997
It has been shown that many proteins, when converted into partially unfolded structures, interact strongly with a lipid bilayer. SecA protein of Escherichia coli is an unusual water-soluble protein which, in the native form, can readily penetrate the membrane and lipid bilayer.
M, Song, H, Kim
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Co-Translational Protein Targeting and Insertion by SecA

2020
Co-translational protein targeting is a conserved process for the biogenesis of membrane proteins. This pathway was generally thought to depend on signal-recognition particle (SRP) for recognition of nascent protein and delivery to the membrane. Recently, SecA was found to also bind ribosomes near the nascent polypeptide exit tunnel, but the function ...
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Structural determinants of SecB recognition by SecA in bacterial protein translocation

Nature Structural & Molecular Biology, 2003
SecB is a bacterial chaperone involved in directing pre-protein to the translocation pathway by its specific interaction with the peripheral membrane ATPase SecA. The SecB-binding site on SecA is located at its C terminus and consists of a stretch of highly conserved residues.
Jiahai, Zhou, Zhaohui, Xu
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Electrophysiological Characterization of SecA-dependent Protein-conducting Channel

2011
Sec translocon is the major machinery for protein translocation in E.coli including SecYEG, SecA and other Sec proteins. It is generally assumed that during translocation process, SecYEG serves as a protein-conducting channel and transports the protein across membranes by using SecA ATPase as driving force. However, previous work suggested that protein
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SecA-like protein-translocating machinery in chloroplasts

Trends in Cell Biology, 1995
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SecA (α) Protein: (seven-component complex)

2008
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