Author： Griffin T.A. Slack J.P. McCluskey T.S. Monaco J.J. Colbert R.A.
Publisher： Academic Press
ISSN： 1522-4724
Source： Molecular Cell Biology Research Communications, Vol.3, Iss.4, 2000-04, pp. : 212-217
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
We have identified a mammalian homologue of yeast Ump1p by searching for similar proteins in human and mouse expressed sequence tag (EST) databases. Ump1p is an accessory protein that is required for normal proteasome assembly in yeast (1). A mammalian homologue, which we refer to as “proteassemblin,” is a constituent of proteasome assembly intermediates (preproteasomes), but not fully assembled 20S proteasomes, as is Ump1p in yeast. We also provide evidence that proteassemblin is a constituent of pre-immunoproteasomes that contain the precursor of the interferon-γ-inducible subunit LMP2. By analogy with Ump1p, we hypothesize that proteassemblin is required for normal mammalian proteasome assembly.
Related content
Access to resources
Recommend
By Groβ Thomas Lutzelberger Martin Wiegmann Holger Klingenhoff Andreas Shenoy Suresh Käufer Norbert F.
Nucleic Acids Research, Vol. 25, Iss. 5, 1997-01 ,pp. :
By Sakumoto N. Yamashita H. Mukai Y. Kaneko Y. Harashima S.
Biochemical and Biophysical Research Communications, Vol. 289, Iss. 2, 2001-11 ,pp. :