退火解旋酶HARP通过与RPA的相互作用被招募到DNA修复位点。
The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA.
作者信息
Yusufzai Timur, Kong Xiangduo, Yokomori Kyoko, Kadonaga James T
机构信息
Section of Molecular Biology, University of California at San Diego, La Jolla, California 92093, USA.
出版信息
Genes Dev. 2009 Oct 15;23(20):2400-4. doi: 10.1101/gad.1831509. Epub 2009 Sep 30.
Abstract
HepA-related protein (HARP) (also known as SMARCAL1) is an ATP-driven annealing helicase that catalyzes the formation of dsDNA from complementary Replication protein A (RPA)-bound ssDNA. Here we find that HARP contains a conserved N-terminal motif that is necessary and sufficient for binding to RPA. This RPA-binding motif is not required for annealing helicase activity, but is essential for the recruitment of HARP to sites of laser-induced DNA damage. These findings suggest that the interaction of HARP with RPA increases the concentration of annealing helicase activity in the vicinity of ssDNA regions to facilitate processes such as DNA repair.
摘要
甲型肝炎相关蛋白（HARP）（也称为SMARCAL1）是一种由ATP驱动的退火解旋酶，可催化由互补的复制蛋白A（RPA）结合的单链DNA形成双链DNA。我们发现HARP含有一个保守的N端基序，该基序对于与RPA结合是必需且足够的。此RPA结合基序对于退火解旋酶活性不是必需的，但对于将HARP募集到激光诱导的DNA损伤位点至关重要。这些发现表明，HARP与RPA的相互作用增加了单链DNA区域附近退火解旋酶活性的浓度，以促进诸如DNA修复等过程。
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