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Published online before print February 6, 2004, 10.1110/ps.03462204
Protein Science (2004), 13:727-734. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila

Moses Makokha1, Yuanpeng Janet Huang2, Gaetano Montelione2, Arthur S. Edison3 and Elisar Barbar1,4

1 Department of Chemistry and Biochemistry, Ohio University, Athens, Ohio 45701-2979, USA
2 Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, New Jersey 08854, USA
3 Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32610-0245, USA

(RECEIVED September 28, 2003; FINAL REVISION November 14, 2003; ACCEPTED November 17, 2003)



Abstract

The structure of Drosophila LC8 pH-induced monomer has been determined by NMR spectroscopy using the program AutoStructure. The structure at pH 3 and 30°C is similar to the individual subunits of mammalian LC8 dimer with the exception that a {beta} strand, which crosses between monomers to form an intersubunit {beta}-sheet in the dimer, is a flexible loop with turnlike conformations in the monomer. Increased flexibility in the interface region relative to the rest of the protein is confirmed by dynamic measurements based on 15N relaxation. Comparison of the monomer and dimer structures indicates that LC8 is not a domain swapped dimer.

Keywords: domain swapping; protein structure; dimerization; dynein light chain; pH-induced dissociation

Reprint requests to: Elisar Barbar, Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA; e-mail: barbare{at}science.oregonstate.edu; fax: (541) 737-0481.

4 Present address: Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR 97331, USA.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03462204.


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