Fig 6.tif (446.86 kB)
Functional complementation of SecA fragments with C-terminal fragment C34.
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posted on 2017-06-02, 17:37 authored by Ying-hsin Hsieh, Ying-ju Huang, Hao Zhang, Qian Liu, Yang Lu, Hsiuchin Yang, John Houghton, Chun Jiang, Sen-Fang Sui, Phang C. Tai(A) Channel activity in SecA domains reconstituted with C34, SecA610-901. (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.
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N 831. SecA domain fragmentsSecA-only protein-conducting channelsion channel activityprotein translocation capabilityN-terminal fragment SecAN 493N-terminal domain fragmentsATPase activityform multi-functional domainsSec-dependent translocation pathwaysN 619-N LipidsSecA domain fragment interactionspore structureform high-efficiency channelsC-terminal deletion fragmentsprotein translocationnon-functional N-terminal fragments643-N901 aminoacyl residuesSecYEG-SecDFprotein translocation abilityform SecA-only pore structuresamino-acyl residues SecA 619-831fragments N 608-NSecA form pore-ring structuresC-terminal fragments complement
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