Novel Function of the Fanconi Anemia Group J or RECQ1 Helicase to Disrupt Protein-DNA Complexes in a Replication Protein A-stimulated Manner

Sommers, Joshua A.; Banerjee, Taraswi; Hinds, Twila; Wan, Bao-Fei; Wold, Marc S.; Lei, Ming; Brosh, Robert M.

doi:10.1074/jbc.m113.542456

Cited by 35 publications

(42 citation statements)

References 81 publications

(82 reference statements)

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“…These data clearly suggest that MtRecG but not MtRuvAB is proficient in reversing the stalled forks that are bound by the KpnI enzyme. Recent study shows that RPA stimulates protein displacement activities of FANCJ or RecQ1 helicase (66). However, such stimulation was not observed with MtSSB when MtRecG/ MtRuvAB-catalyzed fork reversal was tested with KpnI-bound fork structures (data not shown).…”

Section: Tuberculosis Recg But Not Ruvab Efficiently Reverses Modementioning

confidence: 88%

“…However, a similar physical interaction between SSB and RuvAB was not found in their study (83). SSB/RPA has been shown to modulate the activity of various helicases including PriA, RecQ, and FANCJ (66,85,86). Moreover, heterologous SSB proteins have been shown to functionally replace cognate SSBs in RecA-catalyzed strand exchange reactions (37).…”

Section: Discussionmentioning

confidence: 99%

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Mycobacterium tuberculosis RecG Protein but Not RuvAB or RecA Protein Is Efficient at Remodeling the Stalled Replication Forks

Thakur¹,

Basavaraju²,

Khanduja³

et al. 2015

Journal of Biological Chemistry

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Section: Tuberculosis Recg But Not Ruvab Efficiently Reverses Modementioning

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Mycobacterium tuberculosis RecG Protein but Not RuvAB or RecA Protein Is Efficient at Remodeling the Stalled Replication Forks

Thakur¹,

Basavaraju²,

Khanduja³

et al. 2015

Journal of Biological Chemistry

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“…S1) (50). The catalytically inactive BamHI-E111A restriction endonuclease, used in a previous study (32), was provided by New England Biolabs (Ipswich, MA).…”

Section: Methodsmentioning

confidence: 99%

“…The forked duplex DNA substrates with either thymine glycol (Tg) (38) or cyclopurine (cPu) (44) in the helicase translocating or non-translocating strands were prepared as described. The forked duplex substrate harboring a BamHI restriction endonuclease recognition site was prepared as described (32). This same procedure was used to prepare the forked duplex substrate harboring a TFAMbinding site derived from the light strand promoter (5Ј-tgtgttagttggggggtgactgttaaa-3Ј) (53) using the appropriate oligonucleotides shown in supplemental Table S1.…”

Section: Methodsmentioning

confidence: 99%

“…Initially, we tested whether the catalytically inactive BamHI-E111A restriction endonuclease bound to forked duplex substrate with the cognate palindromic BamHI recognition sequence (substrate 27) could inhibit Twinkle-catalyzed unwinding of the DNA substrate. Previously, we had shown that BamHI-E111A bound to the forked duplex substrate potently blocks DNA unwinding of the substrate by the 5Ј to 3Ј FANCJ helicase (32). Using a saturating concentration of BamHI-E111A (38 nM) that we previously determined bound nearly all the forked duplex substrate (32), Twinkle (12 nM) efficiently unwound the BamHI-E111A-bound forked duplex to an extent only slightly less (ϳ8%) than that observed in reactions in which BamHI-E111A was omitted from the reaction mixture (Fig.…”

Section: Twinkle Unwinding and Binding Activity On Replicationmentioning

confidence: 99%

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Biochemical Characterization of the Human Mitochondrial Replicative Twinkle Helicase

Khan

Crouch

Bharti

et al. 2016

Journal of Biological Chemistry

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Mutations in the c10orf2 gene encoding the human mitochondrial DNA replicative helicase Twinkle are linked to several rare genetic diseases characterized by mitochondrial defects. In this study, we have examined the catalytic activity of Twinkle helicase on model replication fork and DNA repair structures. Although Twinkle behaves as a traditional 5 to 3 helicase on conventional forked duplex substrates, the enzyme efficiently dissociates D-loop DNA substrates irrespective of whether it possesses a 5 or 3 single-stranded tailed invading strand. In contrast, we report for the first time that Twinkle branch-migrates an open-ended mobile three-stranded DNA structure with a strong 5 to 3 directionality preference. To determine how well Twinkle handles potential roadblocks to mtDNA replication, we tested the ability of the helicase to unwind substrates with site-specific oxidative DNA lesions or bound by the mitochondrial transcription factor A. Twinkle helicase is inhibited by DNA damage in a unique manner that is dependent on the type of oxidative lesion and the strand in which it resides. Novel single molecule FRET binding and unwinding assays show an interaction of the excluded strand with Twinkle as well as events corresponding to stepwise unwinding and annealing. TFAM inhibits Twinkle unwinding, suggesting other replisome proteins may be required for efficient removal. These studies shed new insight on the catalytic functions of Twinkle on the key DNA structures it would encounter during replication or possibly repair of the mitochondrial genome and how well it tolerates potential roadblocks to DNA unwinding.

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A structural feature of Dda helicase which enhances displacement of streptavidin and trp repressor from DNA

et al. 2021

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Helicases are molecular motors with many activities. They use the energy from ATP hydrolysis to unwind double-stranded nucleic acids while translocating on the single-stranded DNA. In addition to unwinding, many helicases are able to remove proteins from nucleic acids. Bacteriophage T4 Dda is able to displace a variety of DNA binding proteins and streptavidin bound to biotinylated oligonucleotides. We have identified a subdomain of Dda that when deleted, results in a protein variant that has nearly wild type activity for unwinding double-stranded DNA but exhibits greatly reduced streptavidin displacement activity. Interestingly, this domain has little effect on displacement of either gp32 or BamHI bound to DNA but does affect displacement of trp repressor from DNA. With this variant, we have identified residues which enhance displacement of some proteins from DNA.

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Novel Function of the Fanconi Anemia Group J or RECQ1 Helicase to Disrupt Protein-DNA Complexes in a Replication Protein A-stimulated Manner

Cited by 35 publications

References 81 publications

Mycobacterium tuberculosis RecG Protein but Not RuvAB or RecA Protein Is Efficient at Remodeling the Stalled Replication Forks

Mycobacterium tuberculosis RecG Protein but Not RuvAB or RecA Protein Is Efficient at Remodeling the Stalled Replication Forks

Biochemical Characterization of the Human Mitochondrial Replicative Twinkle Helicase

A structural feature of Dda helicase which enhances displacement of streptavidin and trp repressor from DNA

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