Identification and characterization of a mammalian protein interacting with 20S proteasome precursors

被引：77

作者：

Burri, L

Höckendorff, J

Boehm, U

Klamp, T

Dohmen, RJ

Lévy, F ^{[1
]}

机构：

[1] Univ Lausanne, Ludwig Inst Canc Res, Lausanne Branch, CH-1066 Epalinges, Switzerland

[2] Univ Cologne, Inst Genet, D-50674 Cologne, Germany

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2000年 / 97卷 / 19期

关键词：

D O I：

10.1073/pnas.190268597

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 [理学]; 0710 [生物学]; 09 [农学];

摘要：

The assembly of individual mammalian proteasome subunits into catalytically active 20S proteasome is not well understood, Herein, we report the identification and characterization of human and mouse homologues of the yeast proteasome maturating factor Ump1p, We delineate the region of hUMP1 implicated in the specific interaction with proteasome precursors and show that hUMP1 protein is absent from the mature form of the 20S proteasome. We also show that the transcript level of mammalian UMP1 is increased after IFN-gamma treatment and that mammalian UMP1 is functionally related to but not interchangeable with its yeast homologue.

引用

页码：10348 / 10353

页数：6

共 22 条

[1]

Eukaryotic 20S proteasome catalytic subunit propeptides prevent active site inactivation by N-terminal acetylation and promote particle assembly [J].