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Vol. 12, Issue 2, 383-392, February 2001



*Department of Molecular, Cellular, and Developmental Biology, Yale
University, New Haven, Connecticut 06520-8104;
In Arabidopsis seedlings and cauliflower
florets, Rpn6 (a proteasome non-ATPase regulatory subunit) was found in
two distinct protein complexes of ~800 and 500 kDa, respectively. The
large complex likely represents the proteasome 19S regulator particle (RP) because it displays the expected subunit composition and all
characteristics. The small complex, designated PR500, shares at least
three subunits with the "lid" subcomplex of 19S RP and is loosely
associated with an hsp70 protein. In Arabidopsis
COP9 signalosome mutants, PR500 was specifically absent or reduced to
an extent that correlates with the severity of the mutations. Furthermore, PR500 was also diminished in response to potential protein-misfolding stresses caused by the heat shock and canavanine treatment. Immunofluorescence studies suggest that PR500 has a distinct
localization pattern and is enriched in specific nuclear foci. We
propose that PR500 may be evolved in higher plants to cope with the
frequently encountered environmental stresses.
Department of Biochemistry and Cellular and Molecular
Biology, University of Tennessee at Knoxville, Knoxville, Tennessee
37996; and §Cellular and Molecular Biology Program,
University of Wisconsin-Madison, Madison, Wisconsin 53706
Monsanto Company, 700 Chesterfield Parkway North, Mail Code BB3G, St. Louis, MO 63017;
Ceres, Inc., 3007 Malibu Canyon Road, Malibu, CA 90265.
¶
Corresponding author. E-mail address:
xingwang.deng{at}yale.edu.
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