C. Nishimura et al., CDNA CLONING OF RAT PROTEASOME SUBUNIT RC7-I, A HOMOLOG OF YEAST PRE1ESSENTIAL FOR CHYMOTRYPSIN-LIKE ACTIVITY, FEBS letters, 332(1-2), 1993, pp. 52-56
The nucleotide sequence of a cDNA that encodes a new subunit, named RC
7-I, of the 20 S proteasome of rat hepatoma cells has been determined.
The polypeptide predicted from the open reading frame consists of 201
amino acid residues with a calculated molecular weight of 22,912 and
isoelectric point of 7.25. Approximately 80% of the partial amino acid
sequences of several fragments of RC7-I, determined by protein chemic
al analyses, were found to be in excellent accordance with those deduc
ed from the cDNA sequence. Computer analysis showed that RC7-I belongs
to the beta-type subgroup of proteasomes with similarity to the beta-
subunit of the archaebacterial proteasome, differing clearly from alph
a-type subunits of the proteasome gene family. The overall structure o
f RC7-I was found to be homologous to that of yeast PRE1, which is nec
essary for chymotryptic activity.