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J Biol Chem, Vol. 273, Issue 15, 8820-8828, April 10, 1998
B1
From the Department of Cell Biology, Harvard Medical School,
Boston, Massachusetts 02115
Nuclear factor 
B1 (NF-B) is a heterodimeric
complex that regulates transcription of many genes involved in immune
and inflammatory responses. Its 50-kDa subunit (p50) is generated by
the ubiquitin-proteasome pathway from a 105-kDa precursor (p105). We
have reconstituted this proteolytic process in HeLa cell extracts and
purified the responsible enzymes. Ubiquitination of p105 requires E1,
and either of two types of E2s, E2-25K (for which p105 is the first
proven substrate) or a member of the UBCH5 (UBC4) family. It also
requires a new E3 of 50 kDa, which we call E3B. This set of enzymes
differs from the E2s and E3 reported by others to catalyze p105
ubiquitination in reticulocytes. The ubiquitinating enzymes purified
here, together with 26S proteasomes, allowed formation of p50. Thus,
the 26S proteasome provides all the proteolytic activities necessary
for p105 processing. Interestingly, in the reconstituted system, as observed in cells, the C-terminally truncated form of p105, p97, was
processed into p50 more efficiently than normal p105, even when both
species were ubiquitinated to a similar extent. Therefore, some
additional mechanism involving the C-terminal region of p105 influences
the proteolytic processing of the ubiquitinated precursor.
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