Insertion loop‐mediated folding propagation governs efficient maturation of hyperthermophilic Tk‐subtilisin at high temperatures-Reference-Cited by-同舟云学术

Insertion loop‐mediated folding propagation governs efficient maturation of hyperthermophilic Tk‐subtilisin at high temperatures

Published:2020-12-19 Issue:4 Volume:595 Page:452-461
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Lett

Author:

Uehara Ryo¹²³^ORCID,Dan Nanako¹,Amesaka Hiroshi⁴,Yoshizawa Takuya¹,Koga Yuichi⁵,Kanaya Shigenori⁵,Takano Kazufumi⁴,Matsumura Hiroyoshi¹²,Tanaka Shun‐ichi¹²⁴^ORCID

Affiliation:

1. Department of Biotechnology College of Life Sciences Ritsumeikan University Shiga Japan

2. Ritsumeikan Global Innovation Research Organization Ritsumeikan University Shiga Japan

3. Division of Cancer Cell Regulation Aichi Cancer Center Research Institute Nagoya Japan

4. Department of Biomolecular Chemistry Kyoto Prefectural University Japan

5. Department of Material and Life Science Graduate School of Engineering Osaka University Japan

Funder

Japan Society for the Promotion of Science

Hattori Hokokai Foundation

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.14028

Reference39 articles.

1. Active Subtilisin-Like Protease from a Hyperthermophilic Archaeon in a Form with a Putative Prosequence

2. Ca 2+ -Dependent Maturation of Subtilisin from a Hyperthermophilic Archaeon, Thermococcus kodakaraensis : the Propeptide Is a Potent Inhibitor of the Mature Domain but Is Not Required for Its Folding

3. Directed evolution of Tk-subtilisin from a hyperthermophilic archaeon: identification of a single amino acid substitution responsible for low-temperature adaptation

4. Requirement of Left-Handed Glycine Residue for High Stability of the Tk-Subtilisin Propeptide as Revealed by Mutational and Crystallographic Analyses

5. Accelerated maturation of Tk‐subtilisin by a L eu→ P romutation at the C ‐terminus of the propeptide, which reduces the binding of the propeptide to T k‐subtilisin

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