The 20S proteasome is the proteolytic complex that is involved in removing
abnormal proteins and other diverse biological functions. The 20S proteasom
e is constituted of 28 subunits arranged in four rings of seven subunits, a
nd exists as a hollow cylinder. The two outer rings and the two inner rings
are composed of seven different alpha and beta type subunits, respectively
, giving an alpha7 beta7 beta7 alpha7 structure. We previously reported the
primary structures of the 14 proteasomal subunit subfamilies in rice (Oryz
a sativa), representing the first set for all the subfamilies from monocot.
In this study, a distinct cDNA sequence encoding the alpha1 subunit. OsPAA
2, was identified. The amino acid sequence similarity between the two rice
alpha1 subunits was as low as 59.6%, contrasting with those between paralog
s of Arabidopsis proteasome subunit genes. The expression pattern of the Os
PAA2 gene was different from that of another alpha1 gene, OsPAA1. These dat
a suggest that OsPAA2 might play a distinct role from that of OsPAA1 in the
20S proteasome complex. (C) 2001 Published by Elsevier Science B.V. All ri
ghts reserved.