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J. Biol. Chem., Vol. 279, Issue 38, 39251-39259, September 17, 2004

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Oligomeric State of the Escherichia coli Metal Transporter YiiP^*

Yinan Wei, Huilin Li, and Dax Fu

From the Department of Biology, Brookhaven National Laboratory, Upton, New York 11973

YiiP is a 32.9-kDa metal transporter found in the plasma membrane of Escherichia coli (Chao, Y., and Fu, D. (2004) J. Biol. Chem. 279, 17173–17180). Here we report the determination of the YiiP oligomeric state in detergent-lipid micelles and in membranes. Molecular masses of YiiP solubilized with dodecyl-, undecyl-, decyl-, or nonyl--D-maltoside were measured directly using size-exclusion chromatography coupled with laser light-scattering photometry, yielding a mass distribution of YiiP homo-oligomers within a narrow range (68.0–68.8 kDa) that equals the predicted mass of a YiiP dimer within experimental error. The detergent-lipid masses associated with YiiP in the mixed micelles were found to increase from 135.5 to 232.6 kDa, with an apparent correlation with the alkyl chain length of the maltoside detergents. Cross-linking the detergent-solubilized YiiP with 1-ethyl-3-[3-dimethylaminopropyl] carbodiimide hydrochloride (EDC) resulted in a dimeric cross-linked product in an EDC concentration-dependent manner. The oligomeric state of the purified YiiP in reconstituted membranes was determined by electron microscopic analysis of two-dimensional YiiP crystals in negative stain. A projection structure calculated from measurable optical diffractions to 25 Å revealed a pseudo-2-fold symmetry within a molecular boundary of 75 x 40 Å, indicative of the presence of YiiP dimers in membranes. These data provide direct structural evidence for a dimeric association of YiiP both in detergent-lipid micelles and in the reconstituted lipid bilayer. The functional relevance of the dimeric association in YiiP is discussed.

Received for publication, June 23, 2004 , and in revised form, July 14, 2004.

^* This work was supported by the Laboratory-directed Research and Development program of the Brookhaven National Laboratory, Project 02-02 (to D. F.), and by the National Institutes of Health Grant RO1 GM65137 (to D. F.). Brookhaven National Laboratory is managed by Brookhaven Science Associates for the United States Department of Energy. 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.

A Goldhabor post-doctoral fellow.

To whom correspondence should be addressed: Biology Dept., Bldg. 463, Brookhaven National Laboratory, Upton, NY 11973. Tel.: 631-344-4208; Fax: 631-344-3407: E-mail: dax{at}bnl.gov.

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