HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 276, Issue 2, 1383-1390, January 12, 2001

This Article Full Text Full Text (PDF) All Versions of this Article: 276/2/1383    most recent M007379200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Masson, P. Articles by Young, P. Search for Related Content PubMed PubMed Citation Articles by Masson, P. Articles by Young, P. Social Bookmarking                      What's this?

Identification and Characterization of a Drosophila Nuclear Proteasome Regulator
A HOMOLOG OF HUMAN 11 S REG (PA28)^*

Patrick Masson, Oskar Andersson, Ulla-Maja Petersen, and Patrick Young^§

From the Department of Molecular Biology, Stockholm University, S-10691 Stockholm, Sweden

We report the cloning and characterization of a Drosophila proteasome 11 S REG (PA28) homolog. The 28-kDa protein shows 47% identity to the human REG and strongly enhances the trypsin-like activities of both Drosophila and mammalian 20 S proteasomes. Surprisingly, the Drosophila REG was found to inhibit the proteasome's chymotrypsin-like activity against the fluorogenic peptide succinyl-LLVY-7-amino-4-methylcoumarin. Immunocytological analysis reveals that the Drosophila REG is localized to the nucleus but is distributed throughout the cell when nuclear envelope breakdown occurs during mitosis. Through site-directed mutagenesis studies, we have identified a functional nuclear localization signal present in the homolog-specific insert region. The Drosophila PA28 NLS is similar to the oncogene c-Myc nuclear localization motif. Comparison between uninduced and innate immune induced Drosophila cells suggests that the REG proteasome activator has a role independent of the invertebrate immune system. Our results support the idea that  class proteasome activators have an ancient conserved function within metazoans and were present prior to the emergence of the  and  REG classes.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				K. Moriishi, R. Mochizuki, K. Moriya, H. Miyamoto, Y. Mori, T. Abe, S. Murata, K. Tanaka, T. Miyamura, T. Suzuki, et al. Critical role of PA28{gamma} in hepatitis C virus-associated steatogenesis and hepatocarcinogenesis PNAS, January 30, 2007; 104(5): 1661 - 1666. [Abstract] [Full Text] [PDF]

				K. Moriishi, T. Okabayashi, K. Nakai, K. Moriya, K. Koike, S. Murata, T. Chiba, K. Tanaka, R. Suzuki, T. Suzuki, et al. Proteasome Activator PA28{gamma}-Dependent Nuclear Retention and Degradation of Hepatitis C Virus Core Protein J. Virol., October 1, 2003; 77(19): 10237 - 10249. [Abstract] [Full Text] [PDF]

				T. Okamura, S.-i. Taniguchi, T. Ohkura, A. Yoshida, H. Shimizu, M. Sakai, H. Maeta, H. Fukui, Y. Ueta, I. Hisatome, et al. Abnormally High Expression of Proteasome Activator-{gamma} in Thyroid Neoplasm J. Clin. Endocrinol. Metab., March 1, 2003; 88(3): 1374 - 1383. [Abstract] [Full Text] [PDF]