Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer

Citation
L. Jorgensen et Kb. Hendil, Proteasome subunit zeta, a putative ribonuclease, is also found as a free monomer, MOL BIOL RP, 26(1-2), 1999, pp. 119-123
Citations number
23
Categorie Soggetti
Molecular Biology & Genetics
Journal title
MOLECULAR BIOLOGY REPORTS
ISSN journal
03014851 → ACNP
Volume
26
Issue
1-2
Year of publication
1999
Pages
119 - 123
Database
ISI
SICI code
0301-4851(199904)26:1-2<119:PSZAPR>2.0.ZU;2-6
Abstract
20 S Proteasomes are large proteinase complexes found in eukaryotic cells w here they degrade cell proteins in an ATP-dependent manner. Proteasomes con sist of 14 different subunits. One of them, zeta, was found in HeLa cells a t a concentration of 890 mu g per g of cell protein. A large proportion of zeta was found in the free state rather than incorporated into proteasomes, namely 28% in HeLa cells and 37% in BSC-1 cells. Free zeta was found in bo th nuclei and cytoplasm. In HeLa cells free zeta had a t(1/2) of 2.8 h, com pared to 5 d for proteasomes, and did not exchange with zeta in proteasomes . We confirmed (Petit F et al.: Biochem. J. 326: 93-98 (1997)) that both 20 S proteasomes and free zeta subunits possess RNase activity though the act ivities were very low: 4 mMoles and 0.6 mMoles of tobacco mosaic virus RNA degraded per mole of enzyme per min, respectively. The physiological functi on of the relatively abundant zeta monomers is not known.