-
RecA是原核生物体内参与DNA同源识别过程的一种关键蛋白, 长期以来一直是同源重组相关课题的重要研究对象. 通过荧光显微示踪方法, 发现在同源识别过程中 RecA与单链DNA形成的核蛋白丝与模板DNA的结合是短时(τ=0.2 s)和短程(l=1.05 μm)的, 结合后搜寻模板DNA上的同源位点的过程可分为布朗运动和定向运动两种模式. 结合时核蛋白丝并不是缠绕在模板DNA上, 而是以一种更弱的方式结合在模板DNA外侧进行位点搜寻. 如果在该过程中没有找到同源位点, 核蛋白丝就会脱离模板DNA, 并寻找下一次与模板DNA结合的机会, 重复以上过程.
[1] Muskavitch K M T, Linn S 1981 Enzymes 14 233
[2] Maser R S, Monsen K J, Nelms B E, Petrini J H 1997 Mol. Cell. Biol. 17 6087
[3] Benson F E, Stasiak A, West S C 1994 EMBO. J. 13 5764
[4] New J H, Sugiyama T, Zaitseva E, Kowalczykowski S C 1998 Nature 391 407
[5] Constantinou A, Davies A A, West S C 2001 Cell 104 259
[6] Heyer W, Ehmsen K T, Solinger J A 2003 Trends Biochem. Sci. 28 548
[7] Shan Q, Cox M M 1997 J. Biol. Chem. 272 11063
[8] Heijden T V D, Modesti M, Hage S, Kanaar R, Wyman C, Dekker C 2008 Cell 30 530
[9] Joo C, Mckinney S A, Nakamura M, Rasnik I, Myong S, Ha T 2006 Cell 126 515
[10] Forget A L, Kowalczykowski S C 2012 Nature 482 423
[11] Story R M, Weber I T, Steitz T A 1992 Nature 355 318
[12] Tafvizi A, Huang F, Fersht A R, Mirny L A, Oijen A M V 2011 Proc. Natl. Acad. Sci. 108 563
[13] Gorman J, Chowdhury A, Surtees J A, Shimada J, Reichman D R, Alani E, Greene E C 2007 Cell 28 359
[14] Saxton M J, Jacobson K 1997 Annu. Rev. Biophys. Biomol. Struct. 26 373
[15] Graneli A, Yeykal C C, Robertson R B, Greene E C 2006 Proc. Natl. Acad. Sci. 103 1221
[16] Li H, Duan Z W, Dou S X, Wang P Y 2012 Acta Phys. Sin. 61 068701 (in Chinese) [李辉, 段兆文, 窦硕星, 王鹏业 2012 物理学报 61 068701]
[17] Bruinsma R F 2002 Physica A 313 211
[18] Nishinaka T, Shinohara A, Ito Y, Yokoyama S, Shibata T 1998 Proc. Natl. Acad. Sci. 95 11071
[19] Bagchi B, Blainey P C, Xie X S 2008 J. Phys. Chem. B 112 6282
[20] Blainey P C, Luo G B, Kou S C, Mangel W F, Verdine G L, Bagchi B, Xie X S 2009 Nature Struct. Mol. Biol. 16 1224
[21] PHsieh P, Camerini-Otero C S, Camerini-Otero R D 1992 Proc. Natl. Acad. Sci. 89 6492
[22] Rosselli W, Stasiak A 1990 J. Mol. Biol. 216 35
[23] Stasiak A, Capua E D 1982 Nature 299 185
-
[1] Muskavitch K M T, Linn S 1981 Enzymes 14 233
[2] Maser R S, Monsen K J, Nelms B E, Petrini J H 1997 Mol. Cell. Biol. 17 6087
[3] Benson F E, Stasiak A, West S C 1994 EMBO. J. 13 5764
[4] New J H, Sugiyama T, Zaitseva E, Kowalczykowski S C 1998 Nature 391 407
[5] Constantinou A, Davies A A, West S C 2001 Cell 104 259
[6] Heyer W, Ehmsen K T, Solinger J A 2003 Trends Biochem. Sci. 28 548
[7] Shan Q, Cox M M 1997 J. Biol. Chem. 272 11063
[8] Heijden T V D, Modesti M, Hage S, Kanaar R, Wyman C, Dekker C 2008 Cell 30 530
[9] Joo C, Mckinney S A, Nakamura M, Rasnik I, Myong S, Ha T 2006 Cell 126 515
[10] Forget A L, Kowalczykowski S C 2012 Nature 482 423
[11] Story R M, Weber I T, Steitz T A 1992 Nature 355 318
[12] Tafvizi A, Huang F, Fersht A R, Mirny L A, Oijen A M V 2011 Proc. Natl. Acad. Sci. 108 563
[13] Gorman J, Chowdhury A, Surtees J A, Shimada J, Reichman D R, Alani E, Greene E C 2007 Cell 28 359
[14] Saxton M J, Jacobson K 1997 Annu. Rev. Biophys. Biomol. Struct. 26 373
[15] Graneli A, Yeykal C C, Robertson R B, Greene E C 2006 Proc. Natl. Acad. Sci. 103 1221
[16] Li H, Duan Z W, Dou S X, Wang P Y 2012 Acta Phys. Sin. 61 068701 (in Chinese) [李辉, 段兆文, 窦硕星, 王鹏业 2012 物理学报 61 068701]
[17] Bruinsma R F 2002 Physica A 313 211
[18] Nishinaka T, Shinohara A, Ito Y, Yokoyama S, Shibata T 1998 Proc. Natl. Acad. Sci. 95 11071
[19] Bagchi B, Blainey P C, Xie X S 2008 J. Phys. Chem. B 112 6282
[20] Blainey P C, Luo G B, Kou S C, Mangel W F, Verdine G L, Bagchi B, Xie X S 2009 Nature Struct. Mol. Biol. 16 1224
[21] PHsieh P, Camerini-Otero C S, Camerini-Otero R D 1992 Proc. Natl. Acad. Sci. 89 6492
[22] Rosselli W, Stasiak A 1990 J. Mol. Biol. 216 35
[23] Stasiak A, Capua E D 1982 Nature 299 185
| 引用本文: |
|
| Citation: |
|
计量
- 文章访问数: 1399
- PDF下载量: 451
- 被引次数: 0
下载: