Helicase: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs) No edit summary |
Michal Harel (talk | contribs) No edit summary |
||
| (15 intermediate revisions by the same user not shown) | |||
| Line 3: | Line 3: | ||
'''Helicase''' (Hel) is a motor protein which separates nucleic acid strands like DNA double helix or self-annealed RNA. They use ATP hydrolysis for energy. Hel falls into 5 superfamilies (SF1-SF5). Some Hel contain a Helicase and RNase D C terminal | '''Helicase''' (Hel) is a motor protein which separates nucleic acid strands like DNA double helix or self-annealed RNA. They use ATP hydrolysis for energy. Hel falls into 5 superfamilies (SF1-SF5). Some Hel contain a Helicase and RNase D C terminal | ||
Domain (HRDC). The α-thalassemia and mental retardation X-linked syndrome helicase (ATRX ), contains an ATRX-Dnmt3-Dnmt3L (ADD) domain in which many disease-related mutations are found.<br /> | Domain (HRDC). The α-thalassemia and mental retardation X-linked syndrome helicase (ATRX ), contains an ATRX-Dnmt3-Dnmt3L (ADD) domain in which many disease-related mutations are found.<br /> | ||
'''ATP-dependent helicase Rho''' is a protein involved in termination of transcription in prokaryotes. Rho binds to the transcription terminator site on single-stranded RNA. Rho forms a ring-shaped hexamer and advances along the mRNA until it reaches the RNA polymerase and causing it to dissociate from the DNA and end transcription.<br /> | *'''ATP-dependent helicase Rho''' is a protein involved in termination of transcription in prokaryotes. Rho binds to the transcription terminator site on single-stranded RNA. Rho forms a ring-shaped hexamer and advances along the mRNA until it reaches the RNA polymerase and causing it to dissociate from the DNA and end transcription.<br /> | ||
'''ATP-dependent helicase RuvB-like 1''' (RuvBL1) or '''TIP49''' is a human protein which forms hexamers. The hexamer forms dodecamer upon association with RuvBL2 or '''TIP48''' and the complex possesses single-stranded DNA-stimulated ATPase and helicase activities. | *'''ATP-dependent helicase RuvB-like 1''' (RuvBL1) or '''TIP49''' is a human protein which forms hexamers. The hexamer forms dodecamer upon association with RuvBL2 or '''TIP48''' and the complex possesses single-stranded DNA-stimulated ATPase and helicase activities. | ||
*'''ATP-dependent DNA helicase RecG''' or '''RecG''' is an ''E. coli'' protein which acts in recombination and repair of damaged DNA<ref>PMID:8428576</ref> . RecG processes Holliday junctions to mature products. See details in [[RecG Bound to Three-Way DNA Junction]]. | |||
*'''DnaB''' and '''DinG''' exhibit helicase and ATPase activities<ref>PMID:24387047</ref>. | |||
*'''BLM helicase''' or '''Bloom syndrome protein''' can unwind DNA secondary structures<ref>PMID:37503837</ref>. | |||
*'''Sen1 helicese''' has a role in transcription termination of nonpolyadenylated and polyadenylated RNA polymerase II transcripts<ref>PMID:21211720</ref>. | |||
*'''Snf2 helicase''' and '''Swr1 helicase''' regulate the structure and dynamic properties of chromatin<ref>PMID:16738128</ref>. | |||
*'''Ski2 helicase''' is involved in RNA processing and degradation<ref>PMID:22995828</ref>. | |||
*'''XPD helicase''' or '''Rad3''' in yeast is a component of transcription factor IIH<ref>PMID:18510925</ref>. | |||
*'''Cas3 helicase''' exhibits helicase, nuclease and ATPase activities<ref>PMID:25981480</ref>. | |||
*'''Aquarius helicase''' is an RNA helicase that binds pre-mRNA introns to defined position<ref>PMID:25599396</ref>. | |||
For details of PcrA helicase see<br /> | For details of PcrA helicase see<br /> | ||
*[[Molecular Playground/PcrA Helicase]]<br /> | *[[Molecular Playground/PcrA Helicase]]<br /> | ||
| Line 24: | Line 32: | ||
For helicase XPD see<br /> | For helicase XPD see<br /> | ||
*[[XPD Helicase (3CRV)]]<br /> | *[[XPD Helicase (3CRV)]]<br /> | ||
For helicase II or UvrD see<br /> | |||
*[[DNA Repair]]<br /> | |||
For SARS-CoV-2 helicase nsp13 see<br /> | |||
*[[SARS-CoV-2 enzyme Hel]]<br /> | |||
See also<br /> | See also<br /> | ||
*[[Transcription and RNA Processing]] | *[[Transcription and RNA Processing]] | ||
| Line 74: | Line 86: | ||
Betterton MD, Julicher F, "Opening of nucleic-acid double strands by helicases: active versus passive opening.", Physical Review E. 2005 Jan; 71 (1): 011904.<br /> | Betterton MD, Julicher F, "Opening of nucleic-acid double strands by helicases: active versus passive opening.", Physical Review E. 2005 Jan; 71 (1): 011904.<br /> | ||
<ref group="xtra">PMID:16630817</ref><ref group="xtra">PMID:14747711</ref><references group="xtra"/> | <ref group="xtra">PMID:16630817</ref><ref group="xtra">PMID:14747711</ref><references group="xtra"/> | ||
<references/> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
[[Category: Geobacillus stearothermophilus]] | [[Category: Geobacillus stearothermophilus]] | ||
