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Equatorial split of holo‐chaperonin from Thermus thermophilus by ATP and K +
Author(s) -
Ishii Noriyuki,
Taguchi Hideki,
Sasabe Hiroyuki,
Yoshida Masasuke
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00222-u
Subject(s) - thermus thermophilus , chaperonin , thermus , chemistry , thermus aquaticus , biophysics , biochemistry , crystallography , thermophile , biology , protein folding , escherichia coli , enzyme , gene
Holo‐chaperonin molecule from Thermus thermophilus is a bullet‐shaped particle whose cylinder part and round top are composed of two stacked rings of the cpn60 heptamer and a single ring of the cpn10 heptamer, respectively. We found that it splits at the plane between two cpn60 rings into two halves under physiological conditions, that is, in the presence of ATP (but not AMP‐PNP, ADP) + K + (but not Na + ) at 60°C. This equatorial split could be functionally important although it has not been considered in any current mechanistic model of chaperonin functioning.