Ishino So, Kawata Yasushi, Ikegami Takahisa, Matsuzaki Katsumi, Hoshino Masaru
Graduate School of Pharmaceutical Sciences, Kyoto University, 46-29 Yoshida-Shimoadachi, Sakyo-ku, Kyoto 606-8501; Department of Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyama-Minami, Tottori 680-8552; and Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita 565-0871, Japan.
J Biochem. 2014 May;155(5):295-300. doi: 10.1093/jb/mvu009. Epub 2014 Feb 21.
The stability of an SR398/GroES chaperonin complex was examined. As was expected, based on the finding of previous studies, the SR398/GroES complex was extremely stable in the presence of an excess amount of free adenosine 5'-[γ-thio]triphosphate (ATPγS) or adenosine 5'-(β,γ-imido)triphosphate (AMPPNP). However, the complex was not stable in the absence of nucleotides. These results indicate that ATPγS and AMPPNP repeatedly associated to and dissociated from the complex in a non-cooperative manner. This nucleotide exchange did not induce the dissociation of GroES and substrate from SR398, suggesting the importance of the cooperative dissociation of nucleotides from the cis-ring to release GroES and substrate proteins in the GroEL/GroES reaction cycle.
对SR398/GroES伴侣蛋白复合体的稳定性进行了检测。正如基于先前研究结果所预期的那样,在存在过量游离腺苷5'-[γ-硫代]三磷酸(ATPγS)或腺苷5'-(β,γ-亚氨基)三磷酸(AMPPNP)的情况下,SR398/GroES复合体极其稳定。然而,在不存在核苷酸的情况下,该复合体并不稳定。这些结果表明,ATPγS和AMPPNP以非协同方式反复与复合体结合和解离。这种核苷酸交换并未诱导GroES和底物从SR398上解离,这表明在GroEL/GroES反应循环中,核苷酸从顺式环协同解离以释放GroES和底物蛋白具有重要意义。