FEBS Letters | |
MSSP, a protein binding to an origin of replication in the c‐myc gene, interacts with a catalytic subunit of DNA polymerase α and stimulates its polymerase activity | |
Iguchi-Ariga, Sanae M.M.1  Ariga, Hiroyoshi3  Galli, Ivo2  Niki, Takeshi3  | |
[1] College of Medical Technology, Hokkaido University, Kita-ku, Sapporo 060-0812, Japan;Department of Pathology, Stanford University School of Medicine, Stanford, CA 94305-5324, USA;Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita-ku, Sapporo 060-0812, Japan | |
关键词: MSSP; DNA polymerase α; c-myc; | |
DOI : 10.1016/S0014-5793(00)01679-3 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
MSSP has been identified as a protein that binds to both single- and double-stranded sequences of a putative DNA replication origin sequence in the human c-myc gene. MSSP possesses versatile functions, including stimulation of DNA replication, transcriptional regulation, apoptosis induction, and cell transformation coordinated by c-Myc. MSSP contains two RNP domains, RNP1-A and RNP1-B, both of which are necessary for all of the functions of MSSP. In this study, we found that MSSP binds to the N-terminal region of a catalytic subunit of a human DNA polymerase α via its RNP domains both in vitro and in human cells. Furthermore, MSSP was released from the putative DNA replication origin of the c-myc gene after it complexed with DNA polymerase α, and MSSP stimulated DNA polymerase activity in vitro.
【 授权许可】
Unknown
【 预 览 】
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