Gel Immobilization of Acrylamide-Modified Single-Stranded DNA Template for Pyrosequencing

Author(s):  
Pengfeng Xiao ◽  
Huan Huang ◽  
Bingjie Zou ◽  
Qinxin Song ◽  
Guohua Zhou ◽  
...  
1992 ◽  
Vol 12 (7) ◽  
pp. 3216-3223
Author(s):  
S Kornbluth ◽  
C Smythe ◽  
J W Newport

In cell extracts of Xenopus eggs which oscillate between S and M phases of the cell cycle, the onset of mitosis is blocked by the presence of incompletely replicated DNA. In this report, we show that several artificial DNA templates (M13 single-stranded DNA and double-stranded plasmid DNA) can trigger this feedback pathway, which inhibits mitosis. Single-stranded M13 DNA is much more effective than double-stranded plasmid DNA at inhibiting the onset of mitosis. Furthermore, we have shown that low levels of M13 single-stranded DNA and high levels of double-stranded plasmid DNA can elevate the tyrosine kinase activity responsible for phosphorylating p34cdc2, thereby inactivating maturation-promoting factor and inhibiting entry into mitosis. This constitutes a simplified system with which to study the signal transduction pathway from the DNA template to the tyrosine kinase responsible for inhibiting p34cdc2 activity.


2007 ◽  
Vol 28 (12) ◽  
pp. 1903-1912 ◽  
Author(s):  
Pengfeng Xiao ◽  
Huan Huang ◽  
Guohua Zhou ◽  
Zuhong Lu

1987 ◽  
Vol 15 (23) ◽  
pp. 10047-10047 ◽  
Author(s):  
Giannino Del Sal ◽  
Claudio Schneider

DNA Repair ◽  
2009 ◽  
Vol 8 (7) ◽  
pp. 852-856 ◽  
Author(s):  
Kiyonobu Karata ◽  
Antonio E. Vidal ◽  
Roger Woodgate

2021 ◽  
Author(s):  
Qixiang He ◽  
Xiuhua Lin ◽  
Bianca L Chavez ◽  
Benjamin L Lusk ◽  
Ci Ji Lim

Telomere replication and regulation protect mammalian chromosome ends and promote genome stability. An essential step in telomere maintenance is the C-strand fill-in process, which is the de novo synthesis of the complementary strand of the telomere overhang. This step is catalyzed by polymerase-alpha/primase complex (pol-α/primase) and coordinated by an accessory factor, CTC1-STN1-TEN1 (CST). Using cryogenic-electron microscopy single-particle analysis, we report the structure of the human telomere C-strand fill-in preinitiation complex (PIC) at 3.9 Å resolution. The structure reveals a CST and a pol-α/primase co-bound to a single telomere overhang, poised for de novo RNA primer synthesis. Upon PIC assembly, the pol-α/primase undergoes large conformation change from its apo-state; CST partitions the DNA and RNA catalytic centers of pol-α/primase into two separate domains and positions the 3' end of an extended telomere single-stranded DNA template towards the RNA catalytic center (PRIM1 or p49). The telomeric single-stranded DNA template is further positioned by the POLA1 (or p180) catalytically dead exonuclease domain. Together with CST, the exonuclease domain forms a tight-fit molecular tunnel for template direction. Given the structural homology of CST to Replication Protein A (RPA), our structure provides the structural basis for a new model of how pol-α/primase lagging-strand DNA synthesis is coordinated by single-stranded DNA-binding accessory factors.


2011 ◽  
Vol 287 (1) ◽  
pp. 619-627 ◽  
Author(s):  
Hidenori Nakaoka ◽  
Atsuya Nishiyama ◽  
Motoki Saito ◽  
Fuyuki Ishikawa

1998 ◽  
Vol 273 (33) ◽  
pp. 21332-21341 ◽  
Author(s):  
Satoko Maki ◽  
Keiji Hashimoto ◽  
Takeshi Ohara ◽  
Akio Sugino

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