《Nature》目录：2010-06-17出版
时间：2010-06-18 阅读： 我要评论:
http://www.nature.com/nature/journal/v465/n7300/abs/nature09082.html
Article:
http://www.nature.com/nature/journal/v465/n7300/full/nature09082.html
Ubiquitin-dependent DNA damage bypass is separable from genome
replication pp951-955
Post-replicative repair (PRR) enables cells to bypass or overcome DNA damage
during DNA replication. In eukaryotes, ubiquitylation of the replication
clamp PCNA by components of the RAD6 pathway activates damage bypass. When
this occurs has been debated. It is now shown that PRR can be postponed
until much of the undamaged genome is replicated. Moreover, it seems that
PRR occurs mainly by an error-prone process, with error-free bypass playing
a minor role.
Yasukazu Daigaku, Adelina A. Davies and Helle D. Ulrich
doi:10.1038/nature09097
Abstract:
http://www.nature.com/nature/journal/v465/n7300/abs/nature09097.html
Article:
http://www.nature.com/nature/journal/v465/n7300/full/nature09097.html
TFIIA and the transactivator Rap1 cooperate to commit TFIID for
transcription initiation pp956-960
Here, the early steps of activator-dependent transcription in yeast are
examined by using cryo-electron microscopy to study the transcription
activator Rap1 in complex with the general transcription factors TFIID and
TFIIA and with yeast enhancer-promoter DNA. A model is proposed whereby
interactions between Rap1 and TFIIA convey activating signals to TFIID.
Moreover, a Rap1-dependent DNA loop is visualized between the enhancer and
the promoter.
Gabor Papai et al.
doi:10.1038/nature09080
Abstract:
http://www.nature.com/nature/journal/v465/n7300/abs/nature09080.html
Article:
http://www.nature.com/nature/journal/v465/n7300/full/nature09080.html
Structure of the bifunctional isocitrate dehydrogenase
kinase/phosphatase pp961-965
The Escherichia coli isocitrate dehydrogenase kinase/phosphatase (AceK) is a
bifunctional enzyme that can phosphorylate or dephosphorylate isocitrate
dehydrogenase (ICDH) to either inactivate or activate it in response to
environmental changes. Now the structures of AceK and the AceK-ICDH complex
have been solved, revealing the conformational changes that occur when AceK
changes from a kinase to a phosphatase and vice versa.
Jimin Zheng and Zongchao Jia
doi:10.1038/nature09088
Abstract:
http://www.nature.com/nature/journal/v465/n7300/abs/nature09088.html
Article:
Article:
http://www.nature.com/nature/journal/v465/n7300/full/nature09082.html
Ubiquitin-dependent DNA damage bypass is separable from genome
replication pp951-955
Post-replicative repair (PRR) enables cells to bypass or overcome DNA damage
during DNA replication. In eukaryotes, ubiquitylation of the replication
clamp PCNA by components of the RAD6 pathway activates damage bypass. When
this occurs has been debated. It is now shown that PRR can be postponed
until much of the undamaged genome is replicated. Moreover, it seems that
PRR occurs mainly by an error-prone process, with error-free bypass playing
a minor role.
Yasukazu Daigaku, Adelina A. Davies and Helle D. Ulrich
doi:10.1038/nature09097
Abstract:
http://www.nature.com/nature/journal/v465/n7300/abs/nature09097.html
Article:
http://www.nature.com/nature/journal/v465/n7300/full/nature09097.html
TFIIA and the transactivator Rap1 cooperate to commit TFIID for
transcription initiation pp956-960
Here, the early steps of activator-dependent transcription in yeast are
examined by using cryo-electron microscopy to study the transcription
activator Rap1 in complex with the general transcription factors TFIID and
TFIIA and with yeast enhancer-promoter DNA. A model is proposed whereby
interactions between Rap1 and TFIIA convey activating signals to TFIID.
Moreover, a Rap1-dependent DNA loop is visualized between the enhancer and
the promoter.
Gabor Papai et al.
doi:10.1038/nature09080
Abstract:
http://www.nature.com/nature/journal/v465/n7300/abs/nature09080.html
Article:
http://www.nature.com/nature/journal/v465/n7300/full/nature09080.html
Structure of the bifunctional isocitrate dehydrogenase
kinase/phosphatase pp961-965
The Escherichia coli isocitrate dehydrogenase kinase/phosphatase (AceK) is a
bifunctional enzyme that can phosphorylate or dephosphorylate isocitrate
dehydrogenase (ICDH) to either inactivate or activate it in response to
environmental changes. Now the structures of AceK and the AceK-ICDH complex
have been solved, revealing the conformational changes that occur when AceK
changes from a kinase to a phosphatase and vice versa.
Jimin Zheng and Zongchao Jia
doi:10.1038/nature09088
Abstract:
http://www.nature.com/nature/journal/v465/n7300/abs/nature09088.html
Article:
| 《Nature》目录要览 — 2011-04-28出版 |
| 《Nature》目录要览：2011-01-20出版 |
| 《Nature》目录要览：2010-12-23出版 |
| 《Nature》目录要览：2010-12-16出版 |
| 《Nature》目录要览：2010-12-09出版 |
| 《Nature》目录要览：2010-12-02出版 |
特别声明：本文转载仅仅是出于传播信息的需要，版权归原作者所有，并不意味着代表本网站观点或证实其内容的真实性； 如其他媒体、网站或个人从本网站转载使用，须保留本网站注明的“来源”，并自负版权等法律责任； 作者如果不希望被转载或者联系转载稿费等事宜，请与我们接洽：service#environmentor.cn（请将#改为@）。
来源：Nature 作者：Environmentor （环境人 Environmentor.Cn）
