The small heat-shock protein (sHSP) from Methanococcus jannaschii (Mj HSP16.5) forms a homomeric complex of 24 subunits and has an overall structure of a multiwindowed hollow sphere with an external diameter of ≈120 Å and an internal diame...
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https://www.riss.kr/link?id=A60170179
Kim, Rosalind (Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley) ; Luhua Lai (College of Chemistry and Institute of physical Chemistry, Peking University, Beijing, China) ; Lee, Hi-Hong (Department of Biochemistry, Gyeongsang National University, Korea) ; Cheong, Gang-Won (Department of Molecular Cell Biology, Sungkyunkwan University School of Medicine, Korea) ; Kim, Kyeong-Kyu (College of Chemistry and Institute of physical Chemistry, Peking University, Beijing, China) ; Zheng Wu (Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley) ; Hisao Yokota (Department of Molecular and Cell Biology, University of California, Berkeley) ; Susan Marqusee (Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley) ; Kim, Sung-Hou (Department of Chemistry, University of California, 220 Calvin Laboratory, Berkeley)
2003
English
학술저널
111-115(5쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
The small heat-shock protein (sHSP) from Methanococcus jannaschii (Mj HSP16.5) forms a homomeric complex of 24 subunits and has an overall structure of a multiwindowed hollow sphere with an external diameter of ≈120 Å and an internal diame...
The small heat-shock protein (sHSP) from Methanococcus jannaschii (Mj HSP16.5) forms a homomeric complex of 24 subunits and has an overall structure of a multiwindowed hollow sphere with an external diameter of ≈120 Å and an internal diameter of ≈65 Å with six square "windows" of ≈17 Å across and eight triangular windows of ≈30 Å across. This sHSP has been known to protect other proteins from thermal denaturation. Using purified single-chain monellin as a substrate and a series of methods such as protease digestion, antibody binding, and electron microscopy, we show that the substrates bind to Mj HSP16.5 at a high temperature (80℃) on the outside surface of the sphere and are prevented from forming insoluble substrate aggregates in vitro. Circular dichroism studies suggest that a very small, if any, conformational change occurs in sHSP even at 80℃, but substantial conformational changes of the substrate are required for complex formation at 80℃. Furthermore, deletion mutation studies of Mj HSP16.5 suggest that the N-terminal region of the protein has no structural role but may play an important kinetic role in the assembly of the sphere by "preassembly condensation" of multiple monomers before final assembly of the sphere.
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