Functional complementation of SecA fragments with C-terminal fragment C34.
Ying-hsin Hsieh
Ying-ju Huang
Hao Zhang
Qian Liu
Yang Lu
Hsiuchin Yang
John Houghton
Chun Jiang
Sen-Fang Sui
Phang C. Tai
10.1371/journal.pone.0178307.g006
https://plos.figshare.com/articles/figure/Functional_complementation_of_SecA_fragments_with_C-terminal_fragment_C34_/5068711
<p>(A) Channel activity in SecA domains reconstituted with C34, SecA<sub>610-901</sub>. (B) Translocation activity in SecA domains reconstituted with C34. N609 together with C34 have no activity, and could serve as internal negative controls. The reactions were conducted with liposomes with SecYEG or SecYEG-SecDFC as indicated. 100% translocation activity is SecA with SecYEG-DFC.</p>
2017-06-02 17:37:16
N 831. SecA domain fragments
SecA-only protein-conducting channels
ion channel activity
protein translocation capability
N-terminal fragment SecAN 493
N-terminal domain fragments
ATPase activity
form multi-functional domains
Sec-dependent translocation pathways
N 619-N Lipids
SecA domain fragment interactions
pore structure
form high-efficiency channels
C-terminal deletion fragments
protein translocation
non-functional N-terminal fragments
643-N
901 aminoacyl residues
SecYEG-SecDF
protein translocation ability
form SecA-only pore structures
amino-acyl residues SecA 619-831
fragments N 608-N
SecA form pore-ring structures
C-terminal fragments complement