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1 Graduate School of Science and Engineering, Ehime University, Matsuyama, Ehime, Japan;
2 Graduate School of Integrated Science, Yokohama City University, Yokohama, Kanagawa, Japan;
3 Graduate School of Medicine, Osaka City University, Abeno-ku, Osaka, Japan;
4 Integrated Center for Sciences, Ehime University, Matsuyama, Ehime, Japan;
5 Cell-Free Science and Technology Research Center, Ehime University, Matsuyama, Ehime, Japan;
6 Department of Molecular Oncology, Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Tokyo, Japan
Ubiquitination, a modification in which single or multiple ubiquitin molecules are attached to a protein, serves as a signalling function that controls a wide variety of cellular processes. To date, two major forms of polyubiquitin chain have been functionally characterized, in which the isopeptide bond linkages involve Lys48 or Lys63. Lys48-linked polyubiquitin tagging is mostly used to target proteins for degradation by the proteasome, whereas Lys63-linked polyubiquitination has been linked to numerous cellular events that do not rely on degradative signalling via the proteasome. Apparently linkage-specific conformations of polyubiquitin chains are important for these cellular functions, but the structural bases distinguishing Lys48- and Lys63-linked chains remain elusive. Here, we report NMR and small-angle X-ray scattering (SAXS) studies on the intersubunit interfaces and conformations of Lys63- and Lys48-linked di- and tetraubiquitin chains. Our results indicate that, in marked contrast to Lys48-linked chains, Lys63-linked chains are elongated molecules with no stable non-covalent intersubunit interfaces and thus adopt a radically different conformation from that of Lys48-linked chains.
* Correspondence: Email: shirakawa{at}tsurumi.yokohama-cu.ac.jp
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