Effects of divalent cations on encapsulation and release in the GroEL-assisted folding |
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Authors: | Hiroshi Okuda Chihaya Sakuhana Risa Yamamoto Rika Kawai Yuko Mizukami Kazuhiko Matsuda |
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Institution: | (1) Department of Applied Biological Chemistry, School of Agriculture, Kinki University, 3327-204, Nakamachi, Nara 631-8505, Japan |
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Abstract: | Chaperonin GroEL assists protein folding in the presence of ATP and magnesium. Recent studies have shown that several divalent
cations other than magnesium induce conformational changes of GroEL, thereby influencing chaperonin-assisted protein folding,
but little is known about the detailed mechanism for such actions. Thus, the effects of divalent cations on protein encapsulation
by GroEL/ES complexes were investigated. Of the divalent cations, not only magnesium, but also manganese ions enabled the
functional refolding and release of 5,10-methylenetetrahydroforate reductase (METF) by GroEL. Neither ATP hydrolysis nor METF
refolding was observed in the presence of zinc ion, whereas only ATP hydrolysis was induced by cobalt and nickel ions. SDS-PAGE
and gel filtration analyses revealed that cobalt, nickel and zinc ions permit the formation of stable substrate-GroEL-GroES
cis-ternary complexes, but prevent the release of METF from GroEL. |
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Keywords: | GroEL Chaperonin Divalent cation Manganese Cobalt Nickel Zinc Refolding Encapsulation |
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