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20S proteasome from LMP7 knock out mice reveals altered proteolytic activities and cleavage site preferences
Author(s) -
Stohwasser R.,
Kuckelkorn U.,
Kraft R.,
Kostka S.,
Kloetzel P.-M.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00110-x
Subject(s) - cleavage (geology) , proteasome , proteolysis , microbiology and biotechnology , chemistry , gene knockin , biophysics , biochemistry , biology , enzyme , gene , paleontology , fracture (geology)
20S proteasomes of tissues from LMP7 knock out mice which show reduced MHC class I restricted antigen presentation were analyzed with regard to their subunit composition, peptide hydrolyzing activity and their ability to cleave a synthetic 25‐mer polypeptide. LMP7 deficiency results in an enhanced incorporation of subunit MB1 and in a 2–3.8‐fold increase in V max for the Suc‐LLVY‐MCA hydrolyzing activity. Since LMP7 deficiency also affects the cleavage site preference of 20S proteasomes the reduced MHC class I antigen presentation of LMP7 knock out mice is most likely due to an impairment in peptide generation.