FtsH Recognizes Proteins with Unfolded Structure and Hydrolyzes the Carboxyl Side of Hydrophobic Residues.

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概要

• 論文の詳細を見る

• FtsH of Escherichia coli is an essential membrane-integrated ATP-dependent protease. We cloned a gene for an FtsH homolog (T. FtsH) from Thermus thermophilus HB8, expressed it in E. coli, and purified the expressed protein. ATPase activity of T. FtsH was activated by proteins with unfolded structure (α-casein and pepsin), and T. FtsH digested these proteins in an ATP-, Zn2+-dependent manner. α-Lactalbumin was digested by T. FtsH when it was largely unfolded, but not in its native form. Analysis of the proteolytic products revealed that, in most cases, T. FtsH cleaved the C-terminal side of hydrophobic residues and produced a characteristic set of small peptides (<30 kDa) without releasing a large intermediate. Thus, T. FtsH recognizes the unfolded structure of the proteins and progressively digests them at the expense of ATP. A soluble domain of T. FtsH, which lacked the N-terminal two transmembrane helices, was also prepared but was found to retain neither ATPase nor protease activities. Thus, the membrane segment appeared to be indispensable for these activities of T. FtsH.

• 社団法人 日本生化学会の論文

著者

• Yohda Masafumi

  Department Of Biotechnology And Life Science Graduate School Of Engineering Tokyo University Of Agri

• Taguchi Hideki

  Research Laboratory For Surface Science Faculty Of Science Okayama University

• ATSUTA Kyoko

  Research Laboratory of Resources Utilization, Tokyo Institute of Technology

• MOTOHASHI Ken

  Research Laboratory of Resources Utilization, Tokyo Institute of Technology

• Yoshida Masasuke

  Research Lab. Resources Util. Tokyo Inst. Tech.

• Asahara Yuko

  Research Laboratory of Resources Utilization, Tokyo Institute of Technology

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