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Journal of Biochemistry Advance Access published online on July 23, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm144
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© 2007 The Japanese Biochemical Society

Human Geranylgeranyl Diphosphate Synthase Is an Octamer in Solution

Yukino Miyagi, Yoshihiro Matsumura and Hiroshi Sagami

Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577

To whom correspondence should be addressed: H. Sagami, Institute of Multidisciplinary Research for Advanced Materials, Tohoku University, 2-1-1, Katahira, Aoba-ku, Sendai 980-8577, Tel: +81-22-217-5622, Fax: +81-22-217-5620, E-mail: yasagami{at}tagen.tohoku.ac.jp

Received May 9, 2007; Accepted June 17, 2007


  Abstract

A recombinant geranylgeranyl diphosphate synthase (GGPS) was analyzed to be a mixture of octamer, hexamer and dimer by gel filtration using a Superdex 200 column followed by the blue native polyacrylamide gel electrophoresis. The hexamer and dimer were each converted to an octamer by treating with dithiothreitol (DTT). When the recombinant GGPS was preliminarily treated with DTT and similarly analyzed, octamer was predominantly detected with a trace amount of hexamer. The octameric form of GGPS was also supported by the cross-linking experiments with bis(sulfosuccinimidyl) suberate. The GGPS in an octameric form was active with a combination of farnesyl diphosphate and [1-14C]isopentenyl diphosphate. These results indicate that the active form of GGPS in the solution is an octamer rather than hexamer or dimer.

Key Words: cross-linking, geranylgeranyl diphosphate synthase, isoprenylation, prenyltransferase, structure and activity


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