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Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity.
Biochemistry. 2006 Nov 07; 45(44):13401-8.B

Abstract

The YidC protein of Escherichia coli is required for inserting Sec-independent membrane proteins and has a supportive role for the insertion of Sec-dependent proteins into the membrane bilayer. Because a portion of YidC copurifies with the Sec translocase, this interaction might be necessary to assist in the membrane insertion of Sec-dependent proteins. This study describes a deletion analysis that investigates which parts of YidC are required for its interaction with the SecDF complex of the Sec translocase and for the function of YidC as an insertase for the Sec-dependent membrane proteins. The results suggest that the first periplasmic region, which includes residues 24-346, is required for the interaction of YidC with the Sec translocase, in particular with the SecF protein. Further studies showed that residues 215-265 of YidC are sufficient for SecF binding. Surprisingly, the interaction of YidC with SecF is not critical for cell viability as YidC, lacking residues 24-264, was fully functional to support the growth of E. coli. It was also observed that this YidC mutant was fully functional to insert the Sec-dependent subunit A of the F(1)F(o) ATP synthase and an M13 procoat derivative, as well as the Sec-independent M13 procoat protein and subunit C of the ATP synthase. Only when additional residues of the periplasmic region were deleted (265-346) was the membrane insertase function of YidC inhibited.

Authors+Show Affiliations

Department of Chemistry, The Ohio State University, Columbus, Ohio 43210, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17073462

Citation

Xie, Kun, et al. "Different Regions of the Nonconserved Large Periplasmic Domain of Escherichia Coli YidC Are Involved in the SecF Interaction and Membrane Insertase Activity." Biochemistry, vol. 45, no. 44, 2006, pp. 13401-8.
Xie K, Kiefer D, Nagler G, et al. Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity. Biochemistry. 2006;45(44):13401-8.
Xie, K., Kiefer, D., Nagler, G., Dalbey, R. E., & Kuhn, A. (2006). Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity. Biochemistry, 45(44), 13401-8.
Xie K, et al. Different Regions of the Nonconserved Large Periplasmic Domain of Escherichia Coli YidC Are Involved in the SecF Interaction and Membrane Insertase Activity. Biochemistry. 2006 Nov 7;45(44):13401-8. PubMed PMID: 17073462.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Different regions of the nonconserved large periplasmic domain of Escherichia coli YidC are involved in the SecF interaction and membrane insertase activity. AU - Xie,Kun, AU - Kiefer,Dorothee, AU - Nagler,Gisela, AU - Dalbey,Ross E, AU - Kuhn,Andreas, PY - 2006/11/1/pubmed PY - 2006/12/16/medline PY - 2006/11/1/entrez SP - 13401 EP - 8 JF - Biochemistry JO - Biochemistry VL - 45 IS - 44 N2 - The YidC protein of Escherichia coli is required for inserting Sec-independent membrane proteins and has a supportive role for the insertion of Sec-dependent proteins into the membrane bilayer. Because a portion of YidC copurifies with the Sec translocase, this interaction might be necessary to assist in the membrane insertion of Sec-dependent proteins. This study describes a deletion analysis that investigates which parts of YidC are required for its interaction with the SecDF complex of the Sec translocase and for the function of YidC as an insertase for the Sec-dependent membrane proteins. The results suggest that the first periplasmic region, which includes residues 24-346, is required for the interaction of YidC with the Sec translocase, in particular with the SecF protein. Further studies showed that residues 215-265 of YidC are sufficient for SecF binding. Surprisingly, the interaction of YidC with SecF is not critical for cell viability as YidC, lacking residues 24-264, was fully functional to support the growth of E. coli. It was also observed that this YidC mutant was fully functional to insert the Sec-dependent subunit A of the F(1)F(o) ATP synthase and an M13 procoat derivative, as well as the Sec-independent M13 procoat protein and subunit C of the ATP synthase. Only when additional residues of the periplasmic region were deleted (265-346) was the membrane insertase function of YidC inhibited. SN - 0006-2960 UR - https://www.unboundmedicine.com/medline/citation/17073462/Different_regions_of_the_nonconserved_large_periplasmic_domain_of_Escherichia_coli_YidC_are_involved_in_the_SecF_interaction_and_membrane_insertase_activity_ L2 - https://dx.doi.org/10.1021/bi060826z DB - PRIME DP - Unbound Medicine ER -