The linker connecting the tandem ubiquitin binding domains of RAP80 is critical for lysine 63-linked polyubiquitin-dependent binding activity.

Abstract:

:The tandem ubiquitin-interacting motif (UIM) domain located at the N-terminus of Receptor Associated Protein 80 (RAP80) plays a crucial role in ionizing radiation (IR)-induced DNA damage response. RAP80 translocates to sites of IR-induced DNA damage through interaction of its UIM domain with ubiquitinated H2A and Lys63-linked polyubiquitin chains. The exact mechanism, however, through which RAP80 associates with Lys63-linked polyubiquitin chains is not clear. Here, we show by in vitro GST-pull down assays that modifying the linker region between the tandem ubiquitin binding domains of RAP80 changes the binding affinity for Lys63-linked polyubiquitin chains and affects translocation to sites of DNA breaks. Based on these findings, we suggest that the length of the linker region between the tandem ubiquitin binding domains of RAP80 may be a key factor in the binding of RAP80 with Lys63-linked polyubiquitin chains as well as in the translocation of RAP80 to DNA break sites.

journal_name

BMB Rep

journal_title

BMB reports

authors

Cho HJ,Lee S,Kim H

doi

10.5483/bmbrep.2009.42.11.764

subject

Has Abstract

pub_date

2009-11-30 00:00:00

pages

764-8

issue

11

eissn

1976-6696

issn

1976-670X

journal_volume

42

pub_type

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