Abstract
DNA and RNA frequently form various branched intermediates that are important for the transmission of genetic information. Helicases play pivotal roles in the processing of these transient intermediates during nucleic acid metabolism. The archaeal Hef helicase/ nuclease is a representative protein that processes flap- or fork-DNA structures, and, intriguingly, its C-terminal half belongs to the XPF/Mus81 nuclease family. Here, we report the crystal structure of the helicase domain of the Hef protein from Pyrococcus furiosus. The structure reveals a novel helical insertion between the two conserved helicase core domains. This positively charged extra region, structurally similar to the "thumb" domain of DNA polymerase, plays critical roles in fork recognition. The Hef helicase/nuclease exhibits sequence similarity to the Mph1 helicase from Saccharomyces cerevisiae; XPF/Rad1, involved in DNA repair; and a putative Hef homolog identified in mammals. Hence, our findings provide a structural basis for the functional mechanisms of this helicase/nuclease family.
| Original language | English |
|---|---|
| Pages (from-to) | 143-153 |
| Number of pages | 11 |
| Journal | Structure |
| Volume | 13 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - Jan 1 2005 |
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All Science Journal Classification (ASJC) codes
- Structural Biology
- Molecular Biology
Cite this
Crystal structure and functional implications of Pyrococcus furiosus Hef helicase domain involved in branched DNA processing. / Nishino, Tatsuya; Komori, Kayoko; Tsuchiya, Daisuke; Ishino, Yoshizumi; Morikawa, Kosuke.
In: Structure, Vol. 13, No. 1, 01.01.2005, p. 143-153.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Crystal structure and functional implications of Pyrococcus furiosus Hef helicase domain involved in branched DNA processing
AU - Nishino, Tatsuya
AU - Komori, Kayoko
AU - Tsuchiya, Daisuke
AU - Ishino, Yoshizumi
AU - Morikawa, Kosuke
PY - 2005/1/1
Y1 - 2005/1/1
N2 - DNA and RNA frequently form various branched intermediates that are important for the transmission of genetic information. Helicases play pivotal roles in the processing of these transient intermediates during nucleic acid metabolism. The archaeal Hef helicase/ nuclease is a representative protein that processes flap- or fork-DNA structures, and, intriguingly, its C-terminal half belongs to the XPF/Mus81 nuclease family. Here, we report the crystal structure of the helicase domain of the Hef protein from Pyrococcus furiosus. The structure reveals a novel helical insertion between the two conserved helicase core domains. This positively charged extra region, structurally similar to the "thumb" domain of DNA polymerase, plays critical roles in fork recognition. The Hef helicase/nuclease exhibits sequence similarity to the Mph1 helicase from Saccharomyces cerevisiae; XPF/Rad1, involved in DNA repair; and a putative Hef homolog identified in mammals. Hence, our findings provide a structural basis for the functional mechanisms of this helicase/nuclease family.
AB - DNA and RNA frequently form various branched intermediates that are important for the transmission of genetic information. Helicases play pivotal roles in the processing of these transient intermediates during nucleic acid metabolism. The archaeal Hef helicase/ nuclease is a representative protein that processes flap- or fork-DNA structures, and, intriguingly, its C-terminal half belongs to the XPF/Mus81 nuclease family. Here, we report the crystal structure of the helicase domain of the Hef protein from Pyrococcus furiosus. The structure reveals a novel helical insertion between the two conserved helicase core domains. This positively charged extra region, structurally similar to the "thumb" domain of DNA polymerase, plays critical roles in fork recognition. The Hef helicase/nuclease exhibits sequence similarity to the Mph1 helicase from Saccharomyces cerevisiae; XPF/Rad1, involved in DNA repair; and a putative Hef homolog identified in mammals. Hence, our findings provide a structural basis for the functional mechanisms of this helicase/nuclease family.
UR - http://www.scopus.com/inward/record.url?scp=11844252069&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=11844252069&partnerID=8YFLogxK
U2 - 10.1016/j.str.2004.11.008
DO - 10.1016/j.str.2004.11.008
M3 - Article
C2 - 15642269
AN - SCOPUS:11844252069
VL - 13
SP - 143
EP - 153
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 1
ER -