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Papers In Press, published online ahead of print May 6, 2002
J. Biol. Chem, 10.1074/jbc.M203079200
Submitted on March 29, 2002
Revised on May 6, 2002
Accepted on May 6, 2002

A role of the C-terminal region of hRad9 in nuclear transport of the hRad9-hRad1-hHus1 checkpoint complex

Itaru Hirai and Hong-Gang Wang

Drug Discovery Program, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612

Corresponding Author: wanghg{at}moffitt.usf.edu

Rad9, Rad1, and Hus1 are members of the Rad family of checkpoint proteins that are required for both DNA-replication and DNA-damage checkpoints and are thought to function as sensors in the DNA integrity checkpoint control. These proteins can interact with each other and form a stable PCNA-related Rad9-Rad1-Hus1 heterotrimeric complex that might encircle DNA at or near the damaged sites. In this study, we demonstrate that the human Rad9 (hRad9) protein contains a predicted nuclear localization sequence (NLS) near its C-terminus, which plays an essential role in hRad9-mediated G2 checkpoint. Deletion experiments indicate that the NLS-containing region of hRad9 is critical for the nuclear transport of not only hRad9 but also hRad1 and hHus1, although this region is not required for the hRad9-hRad1-hHus1 complex formation. In support of the role that hRad9 NLS plays in the nuclear targeting of the hRad9-hRad1-hHus1 complex, overexpression of a deletion mutant of hRad9 lacking the NLS-containing C-terminal region can bypass the G2 checkpoint and result in cell death after ionizing radiation or hydroxyurea treatment. Moreover, knockdown of hRad9 expression by siRNA results in hRad1 accumulation in the cytoplasm and significantly abrogates the G2 checkpoint in the presence of damaged DNA or incomplete DNA replication. Thus, the C-terminal region of the human Rad9 protein is important for the G2 checkpoint control by operating the transport of the hRad9-hRad1-hHus1 checkpoint complex into the nucleus.


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