JBC Origene Your Gene Company

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on December 17, 2004
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
279/51/53175    most recent
M409243200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Komori, K.
Right arrow Articles by Ishino, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Komori, K.
Right arrow Articles by Ishino, Y.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print October 12, 2004
J. Biol. Chem, 10.1074/jbc.M409243200
Submitted on August 12, 2004
Revised on October 8, 2004
Accepted on October 11, 2004

Cooperation of the N-terminal helicase and C-terminal endonuclease activities of archaeal Hef protein in processing stalled replication fork

Kayoko Komori, Masumi Hidaka, Takashi Horiuchi, Ryosuke Fujikane, Hideo Shinagawa, and Yoshizumi Ishino

Department of Genetic Resources Technology, Kyushu University, Fukuoka, Fukuoka 812-8581

Corresponding Author: ishino{at}agr.kyushu-u.ac.jp

Blockage of replication fork progression often occurs during DNA replication, and repairing and restarting stalled replication forks are essential events in all organisms for the maintenance of genome integrity. The repair system employs processing enzymes to restore the stalled fork. In archaea, Hef is a well-conserved protein that specifically cleaves nicked, flapped, and fork-structured DNAs. This enzyme contains two distinct domains, which are similar to the DEAH helicase family and XPF nuclease superfamily proteins, respectively. Analyses of truncated mutant proteins consisting of each domain revealed that the C-terminal nuclease domain independently recognized and incised fork-structured DNA. The N-terminal helicase domain also specifically unwound fork-structured DNA and Holliday junction DNA in the presence of ATP. Moreover, the endonuclease activity of the whole Hef protein was clearly stimulated by ATP hydrolysis catalyzed by the N-terminal domain. These enzymatic properties suggest that Hef efficiently resolves stalled replication forks by two steps: branch point transfer to the 5-end of the nascent lagging strand, by the N-terminal helicase, followed by template strand incision for leading strand synthesis, by the C-terminal endonuclease.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Cell Biol.Home page
S. Banerjee, S. Smith, J.-H. Oum, H.-J. Liaw, J.-Y. Hwang, N. Sikdar, A. Motegi, S. E. Lee, and K. Myung
Mph1p promotes gross chromosomal rearrangement through partial inhibition of homologous recombination
J. Cell Biol., June 30, 2008; 181(7): 1083 - 1093.
[Abstract] [Full Text] [PDF]

Home page
 Hum Mol GenetHome page
Y. Xue, Y. Li, R. Guo, C. Ling, and W. Wang
FANCM of the Fanconi anemia core complex is required for both monoubiquitination and DNA repair
Hum. Mol. Genet., June 1, 2008; 17(11): 1641 - 1652.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Alpi, F. Langevin, G. Mosedale, Y. J. Machida, A. Dutta, and K. J. Patel
UBE2T, the Fanconi Anemia Core Complex, and FANCD2 Are Recruited Independently to Chromatin: a Basis for the Regulation of FANCD2 Monoubiquitination
Mol. Cell. Biol., December 15, 2007; 27(24): 8421 - 8430.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Sobeck, S. Stone, and M. E. Hoatlin
DNA Structure-Induced Recruitment and Activation of the Fanconi Anemia Pathway Protein FANCD2
Mol. Cell. Biol., June 15, 2007; 27(12): 4283 - 4292.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Kitao, K. Yamamoto, N. Matsushita, M. Ohzeki, M. Ishiai, and M. Takata
Functional Interplay between BRCA2/FancD1 and FancC in DNA Repair
J. Biol. Chem., July 28, 2006; 281(30): 21312 - 21320.
[Abstract] [Full Text] [PDF]

Home page
 GENES CELLSHome page
R. Fujikane, H. Shinagawa, and Y. Ishino
The archaeal Hjm helicase has recQ-like functions, and may be involved in repair of stalled replication fork
Genes Cells, February 1, 2006; 11(2): 99 - 110.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
A. Sobeck, S. Stone, V. Costanzo, B. de Graaf, T. Reuter, J. de Winter, M. Wallisch, Y. Akkari, S. Olson, W. Wang, et al.
Fanconi Anemia Proteins Are Required To Prevent Accumulation of Replication-Associated DNA Double-Strand Breaks
Mol. Cell. Biol., January 15, 2006; 26(2): 425 - 437.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
J. A. Roberts and M. F. White
DNA end-directed and processive nuclease activities of the archaeal XPF enzyme
Nucleic Acids Res., November 27, 2005; 33(20): 6662 - 6670.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2004 by the American Society for Biochemistry and Molecular Biology.