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Purification and Identification of the 20S Proteasome Complex from Zebrafish. | LitMetric

Purification and Identification of the 20S Proteasome Complex from Zebrafish.

Zebrafish

Integrated Bioscience Section, Graduate School of Science and Technology, National University Corporation, Shizuoka University, Shizuoka, Japan.

Published: February 2022

AI Article Synopsis

  • The study focused on purifying the 20S proteasome protein complex from zebrafish, which plays a key role in degrading intracellular proteins.
  • Researchers used a series of five chromatography steps to isolate the 20S proteasome and identified its subunit composition through advanced techniques like mass spectrometry and gel electrophoresis.
  • Notably, the study found 14 different subunits, including two distinct proteins in the α1 subunit and confirmed the presence of the α8 subunit, highlighting specific features of the zebrafish proteasome.

Article Abstract

The proteasome is a large polymeric protease complex responsible for degradation of intracellular proteins and generation of peptides. In this study, we purified a native 20S proteasome protein complex from zebrafish () from the whole body. The cytosolic fraction of zebrafish hydrolyzed Suc-Leu-Leu-Val-Tyr-MCA (Suc-LLVY-MCA), a well-known substrate for the proteasome, in the presence of sodium dodecyl sulfate. From the cytosolic fraction, the 20S proteasome was purified using five column chromatography steps: DEAE cellulose, Q-Sepharose, Sephacryl S-300 gel, hydroxylapatite, and phenyl Sepharose. Electrophoresis and Western blot analyses showed that zebrafish 20S proteasome subunits have molecular masses ranging from 22 to 33 kDa. The subunit composition of the purified 20S proteasome was identified by matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF/MS) analysis after two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) separation. Fourteen kinds of 20S subunits were found. As a special characteristic of zebrafish, two proteins of the α1 subunit were identified. In addition, the results suggested that the α8 subunit is in the 20S complex instead of the α4 subunit. In this study, we demonstrated the subunit composition of the 20S proteasome complex present in zebrafish cells.

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Source
http://dx.doi.org/10.1089/zeb.2021.0064DOI Listing

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