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Defining the regions of Escherichia coli YidC that contribute to activity.
J Biol Chem 2003; 278(49):48965-72JB

Abstract

The YidC/Oxa1/Alb3 family of proteins catalyzes membrane protein insertion in bacteria, mitochondria, and chloroplasts. In this study, we investigated which regions of the bacterial YidC protein are important for its function in membrane protein biogenesis. In Escherichia coli, YidC spans the membrane six times, with a large 319-residue periplasmic domain following the first transmembrane domain. We found that this large periplasmic domain is not required for YidC function and that the residues in the exposed hydrophilic loops or C-terminal tail are not critical for YidC activity. Rather, the five C-terminal transmembrane segments that contain the three consensus sequences in the YidC/Oxa1/Alb3 family are important for its function. However, by systematically replacing all the residues in transmembrane segment (TM) 2, TM3, and TM6 with serine and by swapping TM4 and TM5 with unrelated transmembrane segments, we show that the precise sequence of these transmembrane regions is not essential for in vivo YidC activity. Single serine mutations in TM2, TM3, and TM6 impaired the membrane insertion of the Sec-independent procoat-leader peptidase protein. We propose that the five C-terminal transmembrane segments of YidC function as a platform for the translocating substrate protein to support its insertion into the membrane.

Authors+Show Affiliations

Department of Chemistry, Ohio State University, Columbus, Ohio 43210, USA.No 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
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

14506280

Citation

Jiang, Fenglei, et al. "Defining the Regions of Escherichia Coli YidC That Contribute to Activity." The Journal of Biological Chemistry, vol. 278, no. 49, 2003, pp. 48965-72.
Jiang F, Chen M, Yi L, et al. Defining the regions of Escherichia coli YidC that contribute to activity. J Biol Chem. 2003;278(49):48965-72.
Jiang, F., Chen, M., Yi, L., de Gier, J. W., Kuhn, A., & Dalbey, R. E. (2003). Defining the regions of Escherichia coli YidC that contribute to activity. The Journal of Biological Chemistry, 278(49), pp. 48965-72.
Jiang F, et al. Defining the Regions of Escherichia Coli YidC That Contribute to Activity. J Biol Chem. 2003 Dec 5;278(49):48965-72. PubMed PMID: 14506280.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Defining the regions of Escherichia coli YidC that contribute to activity. AU - Jiang,Fenglei, AU - Chen,Minyong, AU - Yi,Liang, AU - de Gier,Jan-Willem, AU - Kuhn,Andreas, AU - Dalbey,Ross E, Y1 - 2003/09/22/ PY - 2003/9/25/pubmed PY - 2004/3/11/medline PY - 2003/9/25/entrez SP - 48965 EP - 72 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 278 IS - 49 N2 - The YidC/Oxa1/Alb3 family of proteins catalyzes membrane protein insertion in bacteria, mitochondria, and chloroplasts. In this study, we investigated which regions of the bacterial YidC protein are important for its function in membrane protein biogenesis. In Escherichia coli, YidC spans the membrane six times, with a large 319-residue periplasmic domain following the first transmembrane domain. We found that this large periplasmic domain is not required for YidC function and that the residues in the exposed hydrophilic loops or C-terminal tail are not critical for YidC activity. Rather, the five C-terminal transmembrane segments that contain the three consensus sequences in the YidC/Oxa1/Alb3 family are important for its function. However, by systematically replacing all the residues in transmembrane segment (TM) 2, TM3, and TM6 with serine and by swapping TM4 and TM5 with unrelated transmembrane segments, we show that the precise sequence of these transmembrane regions is not essential for in vivo YidC activity. Single serine mutations in TM2, TM3, and TM6 impaired the membrane insertion of the Sec-independent procoat-leader peptidase protein. We propose that the five C-terminal transmembrane segments of YidC function as a platform for the translocating substrate protein to support its insertion into the membrane. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/14506280/Defining_the_regions_of_Escherichia_coli_YidC_that_contribute_to_activity_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=14506280 DB - PRIME DP - Unbound Medicine ER -