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Molecular Chaperones of the Hsp70 Family Interacting with the Proteasome Assembly Network
Author(s) -
Hammack Lindsay J,
Firestone Kyle,
Kusmierczyk Andrew R
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.917.2
Subject(s) - proteasome , hsp90 , chaperone (clinical) , hsp70 , protein folding , atpase , computational biology , microbiology and biotechnology , proteome , chemistry , biochemistry , biology , heat shock protein , gene , enzyme , medicine , pathology
Proteins Ssa1 and Ssa2 are members of the HSP70 family. These nearly identical ATPases are well characterized in maintaining protein homeostasis. Their functions include aiding in protein folding and targeting short‐lived proteins for degradation. These proteins are highly abundant and are routinely detected in mass spectrometry data following affinity purification. However, due to their abundance, these proteins are often assigned to groups of proteins that non‐specifically interact with the purification matrix. Perhaps the best known of these collections is the CRAPome, an online repository of common contaminants found in affinity purification. Even though Ssa1 and Ssa2 are part of the CRAPome, we find that Ssa1/Ssa2 interact with assembling proteasomes, specifically with defined subcomplexes of the core particle. Furthermore, our genetic results also indicate that Ssa1/Ssa2 interact with the with the proteasome assembly network. Proteasome assembly has been characterized as a stepwise process that includes dedicated proteasome assembly chaperones. This work supports an active role for the general molecular chaperones, Ssa1/Ssa2, in this process as well. Support or Funding Information This work was funded in part by a Research Support Funds Grant from IUPUI (to A.R.K.).