E3 ubiquitin liqase activity of the trifunctional ARD1 (ADP-riblosylation factor domain protein 1)

被引:38
作者
Vichi, A [1 ]
Payne, DM [1 ]
Pacheco-Rodriguez, G [1 ]
Moss, J [1 ]
Vaughan, M [1 ]
机构
[1] NHLBI, Pulm Crit Care Med Branch, NIH, Bethesda, MD 20892 USA
关键词
RBCC; TRIM protein; ARF; ARF-GAP;
D O I
10.1073/pnas.0409800102
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 ; 0710 ; 09 ;
摘要
Protein ubiquitinylation plays a key role in many important cellular processes. Ubiquitinylation requires the Ell ubiquitin-activating enzyme, an E2 ubiquitin-conjugating enzyme, and, frequently, a substrate-specific E3 ubiquitin-protein ligase. In one class of E3 ubiquitin ligases, the catalytic domain contains a zinc-binding RING finger motif. ARD1 (ADP-ribosylation factor domain protein 1), with a RING finger domain in the N-terminal region, two predicted B-Boxes, and a coiled-coil protein interaction motif immediately preceding an ADP-ribosylation factor domain at the C terminus, belongs to the TRIM (Tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. The region containing the B-Boxes and the coiled-coil motif acts as a GTPase-activating protein for the ADP-ribosylation factor domain of ARD1. We report here that full-length ARD1 or the RING finger domain (residues 1-110) produced polyubiquitinylated proteins in vitro in the presence of mammalian El, an E2 enzyme (UbcH6 or UbcH5a, -5b, or -5c), ATP, and ubiquitin. Deletion of the RING region or point mutations within the RING sequence abolished ARD1 E3 ligase activity. All data are consistent with a potential function for ARD1 as an E3 ubiquitin ligase in cells.
引用
收藏
页码:1945 / 1950
页数:6
相关论文
共 47 条
[1]   Ubiquitin: not just for proteasomes anymore [J].
Aguilar, RC ;
Wendland, B .
CURRENT OPINION IN CELL BIOLOGY, 2003, 15 (02) :184-190
[2]  
Amerik AY, 1997, EMBO J, V16, P4826
[3]   The herpes simplex virus type 1 (HSV-1) regulatory protein ICP0 interacts with and ubiquitinates p53 [J].
Boutell, C ;
Everett, RD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (38) :36596-36602
[4]  
BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3
[5]   The ret finger protein induces apoptosis via its RING finger-B box-coiled-coil motif [J].
Dho, SH ;
Kwon, KS .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (34) :31902-31908
[6]   An RBCC protein implicated in maintenance of steady-state neuregulin receptor levels [J].
Diamonti, AJ ;
Guy, PM ;
Ivanof, C ;
Wong, K ;
Sweeney, C ;
Carraway, KL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (05) :2866-2871
[7]   Cloning and characterization of a novel RING finger protein that interacts with class V myosins [J].
El-Husseini, AE ;
Vincent, SR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (28) :19771-19777
[8]   SOLUBILIZATION AND PURIFICATION OF ENZYMATICALLY ACTIVE GLUTATHIONE-S-TRANSFERASE (PGEX) FUSION PROTEINS [J].
FRANGIONI, JV ;
NEEL, BG .
ANALYTICAL BIOCHEMISTRY, 1993, 210 (01) :179-187
[9]   Ubiquitination: RING for destruction? [J].
Freemont, PS .
CURRENT BIOLOGY, 2000, 10 (02) :R84-R87
[10]   A NOVEL CYSTEINE-RICH SEQUENCE MOTIF [J].
FREEMONT, PS ;
HANSON, IM ;
TROWSDALE, J .
CELL, 1991, 64 (03) :483-484