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Literature summary for 5.6.2.3 extracted from
- Molecular and cellular functions of the Warsaw breakage syndrome DNA helicase DDX11 (2018), Genes (Basel), 9, 564 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene DDX11, DNA and amino acid sequence determination and analysis | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | in various human cellular systems, DDX11 downregulation by small interfering RNAs (siRNAs) causes a profound delay in mitotic progression leading to chromosome segregation anomalies and sister chromatid cohesion defects | Homo sapiens |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| chromatin | during prophase, DDX11 diffusely coats condensed chromatin | Homo sapiens | 785 | - |
| additional information | during metaphase, DDX11 relocates from chromatids to spindle poles and fibres, and during late telophase, DDX11 accumulates at the midbody | Homo sapiens | - |
- |
| nucleolus | - |
Homo sapiens | 5730 | - |
| nucleus | during interphase, DDX11 has a sparse nuclear localization | Homo sapiens | 5634 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | presence of an iron-sulfur cluster (Fe-S) domain | Homo sapiens |  |
| Mg2+ | required | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Homo sapiens | - |
ADP + phosphate | - |
? | |
| additional information | Homo sapiens | DDX11 is endowed with DNA-dependent ATPase and DNA helicase activities. DDX11 translocates on single-stranded DNA with a 5' to 3' directionality requiring ATP or, to a lesser extent, dATP to fuel this activity. DDX11 DNA strand separation requires a 5'-single-stranded region for helicase loading, since blunt-ended duplex structures do not support DNA unwinding. DDX11 helicase reaction requirements and DNA substrate specificity, overview. DDX11 preferentially unwinds forked duplex DNA substrates with non-complementary 5'- and 3'-single-stranded arms. A 3'-tail having a length between 5- and 10-nt and a 5'-tail of at least 15-nt are required for the helicase to optimally melt double-stranded DNA, duplexes having blunt ends or only a 3'-tail are not unwound. Human DDX11 directly interacts with the Ctf18-replication factor C (RFC) complex, the proliferating cell nuclear antigen (PCNA) factor, and the flap endonuclease 1 (FEN-1) | ? | - |
- |
|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q96FC9 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| C-33A cell | - |
Homo sapiens | - |
| HeLa cell | - |
Homo sapiens | - |
| hTERT-RPE1 cell | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Homo sapiens | ADP + phosphate | - |
? | |
| additional information | DDX11 is endowed with DNA-dependent ATPase and DNA helicase activities. DDX11 translocates on single-stranded DNA with a 5' to 3' directionality requiring ATP or, to a lesser extent, dATP to fuel this activity. DDX11 DNA strand separation requires a 5'-single-stranded region for helicase loading, since blunt-ended duplex structures do not support DNA unwinding. DDX11 helicase reaction requirements and DNA substrate specificity, overview. DDX11 preferentially unwinds forked duplex DNA substrates with non-complementary 5'- and 3'-single-stranded arms. A 3'-tail having a length between 5- and 10-nt and a 5'-tail of at least 15-nt are required for the helicase to optimally melt double-stranded DNA, duplexes having blunt ends or only a 3'-tail are not unwound. Human DDX11 directly interacts with the Ctf18-replication factor C (RFC) complex, the proliferating cell nuclear antigen (PCNA) factor, and the flap endonuclease 1 (FEN-1) | Homo sapiens | ? | - |
- |
|
| additional information | purified recombinant human DDX11 protein possesses ATPase-dependent DNA unwinding activity in vitro. Comprehensive analysis of the DDX11 helicase reaction requirements and DNA substrate specificity, overview | Homo sapiens | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | domain structure, with location of the catalytic core domains HD1 and HD2 (two canonical RecA folds), and three-dimensional structre of DDX11. Structure comparisons, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ATP-dependent DNA helicase | - |
Homo sapiens |
| ChlR1 | - |
Homo sapiens |
| DDX11 | - |
Homo sapiens |
| DNA helicase | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the family of the iron-sulfur cluster containing DNA helicases, and the superfamily 2 (SF2) DNA helicases. SF2 Fe-S DNA helicases play critical functions in the maintenance of genome stability and are linked to rare genetic syndromes and cancer predisposition. An ancestral DDX11 gene might have given rise to a novel family of genes that are characterized by a common subtelomeric location and a similar C-terminal sequence. The function of DDX11 in sister chromatid cohesion establishment appears to be conserved throughout the evolution from yeast to humans | Homo sapiens |
| malfunction | autosomal recessive mutations of the DDX11 gene are responsible for a rare cohesinopathy, a rare genetic disorder named Warsaw breakage syndrome, showing both chromosomal breakages and chromatid cohesion defects. Depletion of either DDX11 or FEN-1 by siRNAs results in cohesion defects in human cells | Homo sapiens |
| metabolism | role of human DDX11 in cellular DNA metabolism and relevant protein interactions, overview. DDX11 is reported to interact with a number of different proteins involved in DNA replication, DNA damage response, sister chromatid cohesion and chromatin architecture and is thought to be a key player in all these important cellular pathways. Human DDX11 directly interacts with and stimulate the enzymatic activity of FEN-1 | Homo sapiens |
| additional information | three-dimensional homology model of DDX11 using as templates both the 10 A resolution cryo-EM structure of human XPD in the TFIIH complex (PDB ID 5IVW), as well as the high resolution crystallographic structure of archaeal XPD enzyme from Thermoplasma acidophilum (PDB ID 4A15) | Homo sapiens |
| physiological function | DDX11 plays multifaceted roles in genome stability maintenance. Potential role of human DDX11 in oncogenesis. DDX11 functions in sister chromatid cohesion, in DNA repair, and in DNA repair and replication fork stabilization, detailed overview. The helicase activity of DDX11 is shown to be capable of displacing duplex regions up to 100 base pairs, which can be extended to 500 base pairs by replication protein A (RPA) or the Ctf18-RFC complex. DDX11 is endowed with DNA-dependent ATPase and DNA helicase activities. DDX11 translocates on single-stranded DNA with a 5' to 3' directionality requiring ATP or, to a lesser extent, dATP to fuel this activity. Moreover, DDX11 DNA strand separation requires a 5'-single-stranded region for helicase loading, since blunt-ended duplex structures do not support DNA unwinding | Homo sapiens |
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