Summary: HRDC domain
This is the Wikipedia entry entitled "RecQ helicase". More...
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RecQ helicase Edit Wikipedia article
|Locus||Chr. 15 |
|RecQ protein-like 4|
|Locus||Chr. 8 q24.3|
|RecQ protein-like 5|
|Locus||Chr. 17 q25|
|RMI1, RecQ mediated genome instability 1|
|Locus||Chr. 9 q22.1|
|Locus||Chr. 8 p|
RecQ helicase is a family of helicase enzymes initially found in Escherichia coli that has been shown to be important in genome maintenance. They function through catalyzing the reaction ATP + H2O → ADP + P and thus driving the unwinding of paired DNA and translocating in the 3' to 5' direction. These enzymes can also drive the reaction NTP + H2O → NDP + P to drive the unwinding of either DNA or RNA.
In prokaryotes RecQ is necessary for plasmid recombination and DNA repair from UV-light, free radicals, and alkylating agents. This protein can also reverse damage from replication errors. In eukaryotes, replication does not proceed normally in the absence of RecQ proteins, which also function in aging, silencing, recombination and DNA repair.
RecQ family members share three regions of conserved protein sequence referred to as the:
- N-terminal – Helicase
- middle – RecQ-conserved (RecQ-Ct) and
- C-terminal – Helicase-and-RNase-D C-terminal (HRDC) domains.
The removal of the N-terminal residues (Helicase and, RecQ-Ct domains) impairs both helicase and ATPase activity but has no effect on the binding ability of RecQ implying that the N-terminus functions as the catalytic end. Truncations of the C-terminus (HRDC domain) compromise the binding ability of RecQ but not the catalytic function. The importance of RecQ in cellular functions is exemplified by human diseases, which all lead to genomic instability and a predisposition to cancer.
There are at least five human RecQ genes; and mutations in three human RecQ genes are implicated in heritable human diseases: WRN gene in Werner syndrome (WS), BLM gene in Bloom syndrome (BS), and RECQ4 in Rothmund-Thomson syndrome. These syndromes are characterized by premature aging, and can give rise to the diseases of cancer, type 2 diabetes, osteoporosis, and atherosclerosis, which are commonly found in old age. These diseases are associated with high incidence of chromosomal abnormalities, including chromosome breaks, complex rearrangements, deletions and translocations, site specific mutations, and in particular sister chromatid exchanges (more common in BS) that are believed to be caused by a high level of somatic recombination.
The proper function of RecQ helicases requires the specific interaction with topoisomerase III (Top 3). Top 3 changes the topological status of DNA by binding and cleaving single stranded DNA and passing either a single stranded or a double stranded DNA segment through the transient break and finally religating the break. The interaction of RecQ helicase with topoisomerase III at the N-terminal region is involved in the suppression of spontaneous and damage induced recombination and the absence of this interaction results in a lethal or very severe phenotype. The emerging picture clearly is that RecQ helicases in concert with Top 3 are involved in maintaining genomic stability and integrity by controlling recombination events, and repairing DNA damage in the G2-phase of the cell cycle. The importance of RecQ for genomic integrity is exemplified by the diseases that arise as a consequence of mutations or malfunctions in RecQ helicases; thus it is crucial that RecQ is present and functional to ensure proper human growth and development.
- Bernstein DA, Keck JL (June 2003). "Domain mapping of Escherichia coli RecQ defines the roles of conserved N- and C-terminal regions in the RecQ family". Nucleic Acids Res. 31 (11): 2778–85. doi:10.1093/nar/gkg376. PMC 156711. PMID 12771204.
- Cobb JA, Bjergbaek L, Gasser SM (October 2002). "RecQ helicases: at the heart of genetic stability". FEBS Lett. 529 (1): 43–8. doi:10.1016/S0014-5793(02)03269-6. PMID 12354611.
- Kaneko H, Fukao T, Kondo N (2004). "The function of RecQ helicase gene family (especially BLM) in DNA recombination and joining". Adv. Biophys. 38: 45–64. doi:10.1016/S0065-227X(04)80061-3. PMID 15493327.
- Ouyang KJ, Woo LL, Ellis NA (2008). "Homologous recombination and maintenance of genome integrity: cancer and aging through the prism of human RecQ helicases". Mech. Ageing Dev. 129 (7-8): 425–40. doi:10.1016/j.mad.2008.03.003. PMID 18430459.
- Hanada K, Hickson ID (September 2007). "Molecular genetics of RecQ helicase disorders". Cell. Mol. Life Sci. 64 (17): 2306–22. doi:10.1007/s00018-007-7121-z. PMID 17571213.
- Skouboe C, Bjergbaek L, Andersen AH (2005). "Genome instability as a cause of ageing and cancer: Implications of RecQ helicases". Signal Transduction 5 (3): 142–151. doi:10.1002/sita.200400052.
- Laursen LV, Bjergbaek L, Murray JM, Andersen AH (2003). "RecQ helicases and topoisomerase III in cancer and aging". Biogerontology 4 (5): 275–87. doi:10.1023/A:1026218513772. PMID 14618025.
- RecQ Helicases, introduction at UNC's Sekelsky Lab.
- BLM gene encodes a RecQ Helicase, description of the gene
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HRDC domain Provide feedback
The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain cause human disease. It is interesting to note that the RecQ helicase in Deinococcus radiodurans has three tandem HRDC domains .
Wu L, Chan KL, Ralf C, Bernstein DA, Garcia PL, Bohr VA, Vindigni A, Janscak P, Keck JL, Hickson ID; , EMBO J. 2005;24:2679-2687.: The HRDC domain of BLM is required for the dissolution of double Holliday junctions. PUBMED:15990871 EPMC:15990871
Liu Z, Macias MJ, Bottomley MJ, Stier G, Linge JP, Nilges M, Bork P, Sattler M; , Structure. 1999;7:1557-1566.: The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins. PUBMED:10647186 EPMC:10647186
Huang L, Hua X, Lu H, Gao G, Tian B, Shen B, Hua Y; , DNA Repair (Amst). 2006; [Epub ahead of print]: Three tandem HRDC domains have synergistic effect on the RecQ functions in Deinococcus radiodurans. PUBMED:17085080 EPMC:17085080
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002121The HRDC (Helicase and RNase D C-terminal) domain has a putative role in nucleic acid binding. Mutations in the HRDC domain associated with the human BLM gene result in Bloom Syndrome (BS), an autosomal recessive disorder characterised by proportionate pre- and postnatal growth deficiency; sun-sensitive, telangiectatic, hypo- and hyperpigmented skin; predisposition to malignancy; and chromosomal instability [PUBMED:9397680].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||intracellular (GO:0005622)|
|Molecular function||nucleic acid binding (GO:0003676)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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Superfamily includes HRDC domain from helicases, RNA polymerase II subunit RBP4, RNase D C-terminal domains, and EXOSC10 HRDC domain-like families.
The clan contains the following 3 members:Helicase_Sgs1 HRDC RNA_pol_Rpb4
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Number in seed:||147|
|Number in full:||6087|
|Average length of the domain:||67.30 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||11.64 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||18|
|Download:||download the raw HMM for this family|
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the HRDC domain has been found. There are 22 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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