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Reconstitution of functionally efficient SecA-dependent protein-conducting channels: transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels.
Biochem Biophys Res Commun 2013; 431(3):388-92BB

Abstract

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 same as those of native membranes, indicating the transformation of reconstituted functional high-affinity protein-conducting channels from the low-affinity SecA-channels.

Authors+Show Affiliations

Department of Biology and Center of Biotechnology and Drug Design, Georgia State University, Atlanta, GA 30303, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

23337498

Citation

Hsieh, Ying-hsin, et al. "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, vol. 431, no. 3, 2013, pp. 388-92.
Hsieh YH, Zhang H, Wang H, et al. Reconstitution of functionally efficient SecA-dependent protein-conducting channels: transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels. Biochem Biophys Res Commun. 2013;431(3):388-92.
Hsieh, Y. H., Zhang, H., Wang, H., Yang, H., Jiang, C., Sui, S. F., & Tai, P. C. (2013). 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, 431(3), pp. 388-92. doi:10.1016/j.bbrc.2013.01.042.
Hsieh YH, et al. Reconstitution of Functionally Efficient SecA-dependent Protein-conducting Channels: Transformation of Low-affinity SecA-liposome Channels to High-affinity SecA-SecYEG-SecDF·YajC Channels. Biochem Biophys Res Commun. 2013 Feb 15;431(3):388-92. PubMed PMID: 23337498.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Reconstitution of functionally efficient SecA-dependent protein-conducting channels: transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels. AU - Hsieh,Ying-hsin, AU - Zhang,Hao, AU - Wang,Hongyun, AU - Yang,Hsiuchin, AU - Jiang,Chun, AU - Sui,Sen-fang, AU - Tai,Phang C, Y1 - 2013/01/18/ PY - 2012/12/27/received PY - 2013/01/10/accepted PY - 2013/1/23/entrez PY - 2013/1/23/pubmed PY - 2013/8/28/medline SP - 388 EP - 92 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 431 IS - 3 N2 - 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 same as those of native membranes, indicating the transformation of reconstituted functional high-affinity protein-conducting channels from the low-affinity SecA-channels. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/23337498/Reconstitution_of_functionally_efficient_SecA_dependent_protein_conducting_channels:_transformation_of_low_affinity_SecA_liposome_channels_to_high_affinity_SecA_SecYEG_SecDF·YajC_channels_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(13)00108-3 DB - PRIME DP - Unbound Medicine ER -