Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr

10.1038/4220 ◽  
1998 ◽  
Vol 5 (12) ◽  
pp. 1042-1047 ◽  
Author(s):  
Thorsten Dieckmann ◽  
Elizabeth S. Withers-Ward ◽  
Mark A. Jarosinski ◽  
Chuan-Fa Liu ◽  
Irvin S. Y. Chen ◽  
...  
Keyword(s):  
Dna Repair ◽  
Human Dna ◽  
Repair Protein ◽  
Uba Domain ◽  
Dna Repair Protein ◽  
Hiv 1

Domain Mapping of the DNA Binding, Endonuclease, and ERCC1 Binding Properties of the Human DNA Repair Protein XPF†

Biochemistry ◽  
1999 ◽  
Vol 38 (29) ◽  
pp. 9417-9425 ◽  
Author(s):  
Sandra L. McCutchen-Maloney ◽  
Cindi A. Giannecchini ◽  
Mona H. Hwang ◽  
Michael P. Thelen
Keyword(s):  
Dna Repair ◽  
Dna Binding ◽  
Binding Properties ◽  
Human Dna ◽  
Repair Protein ◽  
Domain Mapping ◽  
Dna Repair Protein

scholarly journals Noncovalent Interaction between Ubiquitin and the Human DNA Repair Protein Mms2 Is Required for Ubc13-mediated Polyubiquitination

2001 ◽  
Vol 276 (43) ◽  
pp. 40120-40126 ◽  
Author(s):  
Sean McKenna ◽  
Leo Spyracopoulos ◽  
Trevor Moraes ◽  
Landon Pastushok ◽  
Christopher Ptak ◽  
...  
Keyword(s):  
Dna Repair ◽  
Noncovalent Interaction ◽  
Human Dna ◽  
Repair Protein ◽  
Dna Repair Protein

scholarly journals Suppression of UV-induced apoptosis by the human DNA repair protein XPG

2005 ◽  
Vol 13 (3) ◽  
pp. 478-488 ◽  
Author(s):  
V Clément ◽  
I Dunand-Sauthier ◽  
S G Clarkson
Keyword(s):  
Dna Repair ◽  
Human Dna ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Induced Apoptosis

scholarly journals Biphasic Kinetics of the Human DNA Repair Protein MED1 (MBD4), a Mismatch-specific DNAN-Glycosylase

2000 ◽  
Vol 275 (42) ◽  
pp. 32422-32429 ◽  
Author(s):  
Fiorella Petronzelli ◽  
Antonio Riccio ◽  
George D. Markham ◽  
Steven H. Seeholzer ◽  
Jay Stoerker ◽  
...  
Keyword(s):  
Dna Repair ◽  
Biphasic Kinetics ◽  
Human Dna ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Kinetics Of

scholarly journals Involvement of the DNA Repair Protein hHR23 inp53Degradation

2003 ◽  
Vol 23 (24) ◽  
pp. 8960-8969 ◽  
Author(s):  
Sandra Glockzin ◽  
Francois-Xavier Ogi ◽  
Arnd Hengstermann ◽  
Martin Scheffner ◽  
Christine Blattner
Keyword(s):  
Dna Repair ◽  
26S Proteasome ◽  
Polyubiquitin Chains ◽  
Proteolytic Pathway ◽  
Repair Protein ◽  
Uba Domain ◽  
Dna Repair Protein ◽  
The Stability

ABSTRACT The stability of the tumor suppressor protein p53 is regulated via the ubiquitin-proteasome-dependent proteolytic pathway. Like most substrates of this pathway, p53 is modified by the attachment of polyubiquitin chains prior to proteasome-mediated degradation. However, the mechanism(s) involved in the delivery of polyubiquitylated p53 molecules to the proteasome are currently unclear. Here, we show that the human DNA repair protein hHR23 binds to polyubiquitylated p53 via its carboxyl-terminal ubiquitin-associated (Uba) domain shielding p53 from deubiquitylation in vitro and in vivo. In addition, downregulation of hHR23 expression within cells by RNA interference results in accumulation of p53. Since the Ubl domain of hHR23 has been shown to interact with the 26S proteasome, we propose that hHR23 is intrinsically involved in the delivery of polyubiquitylated p53 molecules to the proteasome. In this model, the Uba domain of hHR23 binds to polyubiquitin chains formed on p53 and protects them from deubiquitylation, while the Ubl domain delivers the polyubiquitylated p53 molecules to the proteasome.

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