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Delta-aminolevulinic dehydratase is a proteasome interacting protein.

Authors: Bardag-Gorce, Fawzia  French, Samuel W 
Citation: Bardag-Gorce F and French SW, Exp Mol Pathol. 2011 Oct;91(2):485-9. doi: 10.1016/j.yexmp.2011.05.003. Epub 2011 May 27.
Pubmed: (View Article at PubMed) PMID:21640720
DOI: Full-text: DOI:10.1016/j.yexmp.2011.05.003

The proteasome interacts with a large number of proteins which regulate specific cellular functions. The focus of this study is to examine the proteasome interaction with Delta-aminolevulinate dehydratase (ALAD). ALAD is involved in the heme biosynthesis pathway and was co-isolated, with the 20S proteasome using several chromatographic purification steps. The MALDI-TOF mass spectrometry analysis identified this proteasome co-isolated protein as ALAD. When the proteasome was isolated using density-gradient centrifugation, ALAD was also found in the 26S proteasome fractions. It co-isolated with the 20S more than with the 26S proteasome. Furthermore, immunoprecipitated ALAD stained positive with antibodies to proteasome subunits. These results indicate that ALAD might interact with the proteasome. It is possible that ALAD is involved in modulating proteasome activity. When purified proteasomes were incubated with ALAD it was found that ALAD changes proteasome activity in a dose dependent manner. This indicates that ALAD may play a significant role in regulating proteasome activity. The data supports the hypothesis that ALAD, an important enzyme for heme synthesis, is also important as a proteasome interacting protein.


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CRRD Object Information
CRRD ID: 12904696
Created: 2017-05-17
Species: All species
Last Modified: 2017-05-17
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.