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J. Biol. Chem., Vol. 278, Issue 26, 23295-23300, June 27, 2003

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Conditional Lethal Mutations Separate the M13 Procoat and Pf3 Coat Functions of YidC

DIFFERENT YIDC STRUCTURAL REQUIREMENTS FOR MEMBRANE PROTEIN INSERTION^*

Minyong Chen , Kun Xie , Nico Nouwen , Arnold J. M. Driessen  and Ross E. Dalbey  ¶

From the Department of Chemistry and Biochemistry Program, The Ohio State University, Columbus, Ohio 43210 and the Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands

Conditional lethal YidC mutants have been isolated to decipher the role of YidC in the assembly of Sec-dependent and Sec-independent membrane proteins. We now show that the membrane insertion of the Sec-independent M13 procoat-lep protein is inhibited in a short time in a temperature-sensitive mutant when shifted to the nonpermissive temperature. This provides an additional line of evidence that YidC plays a direct role in the insertion of the Sec-independent M13 procoat protein. However, in the temperature-sensitive mutant, the insertion of the Sec-independent Pf3 phage coat protein and the Sec-dependent leader peptidase were not strongly inhibited at the restricted temperatures. Conversely, using a cold-sensitive YidC strain, we find that the membrane insertion of the Sec-independent Pf3 coat protein is blocked, and the Sec-dependent leader peptidase is inhibited at the nonpermissive temperature, whereas the insertion of the M13 procoat protein is nearly normal. These data show that the YidC function for procoat and its function for Pf3 coat and possibly leader peptidase are genetically separable and suggest that the YidC structural requirements are different for the Sec-independent M13 procoat and Pf3 coat phage proteins that insert by different mechanisms.

Received for publication, January 30, 2003 , and in revised form, April 15, 2003.

^* This work was supported by National Institutes of Health Grant GM63862 (to R. E. D.) and by funds from the Council for Chemical Sciences of the Netherlands Organization for Scientific Research and the Dutch Organization for the Advancement of Scientific Research (to A. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Tel.: 614-292-2384; Fax: 614-292-1532; E-mail: dalbey{at}chemistry.ohio-state.edu.

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