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Related Experiment Videos

A proteasome activator subunit binds calcium

C Realini1, M Rechsteiner

  • 1Department of Biochemistry, University of Utah School of Medicine, Salt Lake City 84132, USA.

The Journal of Biological Chemistry
|December 15, 1995
PubMed
Summary
This summary is machine-generated.

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The 29-kDa regulator (REG) subunit of human red blood cells binds calcium ions (Ca2+). This calcium binding reversibly inhibits protease activity, suggesting calcium may regulate protease function in vivo.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The 29-kDa subunit of human red blood cell regulator (REG) activates the multicatalytic protease.
  • REG subunit's sequence features a motif of alternating lysine and glutamic acid residues (KEKE).
  • Similar motifs are found in calcium-binding proteins.

Purpose of the Study:

  • To investigate the calcium-binding properties of the 29-kDa REG subunit.
  • To determine if the KEKE motif is responsible for calcium binding.
  • To explore the effect of calcium on the REG subunit's interaction with the multicatalytic protease.

Main Methods:

  • Cloning of cDNA encoding the 29-kDa REG subunit.
  • Recombinant protein expression and purification.

Related Experiment Videos

  • Filter assays using 45Ca2+ and ruthenium red to assess calcium binding.
  • Analysis of protease activity in the presence of calcium.

    • Main Results:

    • The recombinant 29-kDa REG subunit binds 45Ca2+ and ruthenium red.
    • A ubiquitin extension protein containing the KEKE region also binds 45Ca2+.
    • Calcium (Ca2+) reversibly inhibits the peptidase activity of REG-protease complexes.

    Conclusions:

    • The 29-kDa REG subunit is a calcium-binding protein.
    • The KEKE region within the REG subunit mediates divalent cation binding.
    • Multicatalytic protease activity may be regulated by calcium in vivo.