小鼠端粒DNA的四链体结构与小鼠端粒结合蛋白Pot1的端粒DNA结合结构域之间的相互作用。

Interaction between tetraplex structure of mouse telomeric DNA and telomeric DNA binding domains of mouse telomere binding protein Pot1.

作者信息

Kaneda Kaoru, Torigoe Hidetaka

机构信息

Department of Applied Chemistry, Faculty of Science, Tokyo University of Science, Tokyo 162-8601, Japan.

出版信息

Nucleic Acids Symp Ser (Oxf). 2009(53):245-6. doi: 10.1093/nass/nrp123.

DOI:10.1093/nass/nrp123

PMID:19749352

Abstract

Mouse telomeric DNA sequence, Tel3.5: 5'-AGGG(T TAGGG)(3)-3', has the ability to form antiparallel tetraplex structure in the presence of Na(+). We examined the interaction between the antiparallel tetraplex structure of Tel3.5 and each of two single-stranded telomeric DNA-binding domains of mouse telomere binding protein Pot1, mPot1OB1 and mPot1OB2. The antiparallel tetraplex of Tel3.5 became unfolded upon the interaction with mPot1OB1. On the other hand, no significant structural change of the antiparallel tetraplex of Tel3.5 was observed upon the interaction with mPot1OB2. Considering that the antiparallel tetraplex inhibits telomerase-mediated telomere elongation, we conclude that the ability of mPot1OB1 to unfold the antiparallel tetraplex of the mouse telomeric DNA is required for telomerase-mediated telomere elongation.

摘要

小鼠端粒DNA序列Tel3.5：5'-AGGG(T TAGGG)(3)-3'，在存在Na(+)的情况下能够形成反平行四链体结构。我们研究了Tel3.5的反平行四链体结构与小鼠端粒结合蛋白Pot1的两个单链端粒DNA结合结构域mPot1OB1和mPot1OB2之间的相互作用。Tel3.5的反平行四链体在与mPot1OB1相互作用时发生解折叠。另一方面，在与mPot1OB2相互作用时，未观察到Tel3.5的反平行四链体有明显的结构变化。鉴于反平行四链体抑制端粒酶介导的端粒延长，我们得出结论，端粒酶介导的端粒延长需要mPot1OB1解开小鼠端粒DNA反平行四链体的能力。