scholarly journals PICH: A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA

2013 ◽  
Vol 51 (5) ◽  
pp. 691-701 ◽  
Author(s):  
Andreas Biebricher ◽  
Seiki Hirano ◽  
Jacqueline H. Enzlin ◽  
Nicola Wiechens ◽  
Werner W. Streicher ◽  
...  
Keyword(s):  
Anaphase Bridge ◽  
Dna Translocase

How Chi Sequence Modifies RecBCD Single-Stranded DNA Translocase Activity

ChemPhysChem ◽  
2017 ◽  
Vol 19 (2) ◽  
pp. 243-247 ◽  
Author(s):  
Chia-Chuan Cho ◽  
Cinya Chung ◽  
Hung-Wen Li
Keyword(s):  
Single Stranded Dna ◽  
Chi Sequence ◽  
Dna Translocase

scholarly journals Evidence that the SpoIIIE DNA translocase participates in membrane fusion during cytokinesis and engulfment

2006 ◽  
Vol 59 (4) ◽  
pp. 1097-1113 ◽  
Author(s):  
Nai-Jia Linda Liu ◽  
Rachel J. Dutton ◽  
Kit Pogliano
Keyword(s):  
Membrane Fusion ◽  
Dna Translocase

scholarly journals RAD54 is essential for RAD51-mediated repair of meiotic DSB in Arabidopsis

PLoS Genetics ◽  
2021 ◽  
Vol 17 (5) ◽  
pp. e1008919
Author(s):  
Miguel Hernandez Sanchez-Rebato ◽  
Alida M. Bouatta ◽  
Maria E. Gallego ◽  
Charles I. White ◽  
Olivier Da Ines
Keyword(s):  
Homologous Recombination ◽  
Meiotic Recombination ◽  
Dna Supercoiling ◽  
Homology Search ◽  
Detectable Effect ◽  
Damage Repair ◽  
Meiotic Dsbs ◽  
Dna Translocase

An essential component of the homologous recombination machinery in eukaryotes, the RAD54 protein is a member of the SWI2/SNF2 family of helicases with dsDNA-dependent ATPase, DNA translocase, DNA supercoiling and chromatin remodelling activities. It is a motor protein that translocates along dsDNA and performs multiple functions in homologous recombination. In particular, RAD54 is an essential cofactor for regulating RAD51 activity. It stabilizes the RAD51 nucleofilament, remodels nucleosomes, and stimulates homology search and strand invasion activity of RAD51. Accordingly, deletion of RAD54 has dramatic consequences on DNA damage repair in mitotic cells. In contrast, its role in meiotic recombination is less clear. RAD54 is essential for meiotic recombination in Drosophila and C. elegans, but plays minor roles in yeast and mammals. We present here characterization of the roles of RAD54 in meiotic recombination in the model plant Arabidopsis thaliana. Absence of RAD54 has no detectable effect on meiotic recombination in otherwise wild-type plants but RAD54 becomes essential for meiotic DSB repair in absence of DMC1. In Arabidopsis, dmc1 mutants have an achiasmate meiosis, in which RAD51 repairs meiotic DSBs. Lack of RAD54 leads to meiotic chromosomal fragmentation in absence of DMC1. The action of RAD54 in meiotic RAD51 activity is thus mainly downstream of the role of RAD51 in supporting the activity of DMC1. Equivalent analyses show no effect on meiosis of combining dmc1 with the mutants of the RAD51-mediators RAD51B, RAD51D and XRCC2. RAD54 is thus required for repair of meiotic DSBs by RAD51 and the absence of meiotic phenotype in rad54 plants is a consequence of RAD51 playing a RAD54-independent supporting role to DMC1 in meiotic recombination.

scholarly journals High-Throughput Screening to Identify Inhibitors of DEAD Box Helicase DDX41

2017 ◽  
Vol 22 (9) ◽  
pp. 1084-1092 ◽  
Author(s):  
Mariko Yoneyama-Hirozane ◽  
Mitsuyo Kondo ◽  
Shin-ichi Matsumoto ◽  
Akiko Morikawa-Oki ◽  
Daisuke Morishita ◽  
...  
Keyword(s):  
High Throughput ◽  
High Throughput Screening ◽  
Acute Myelocytic Leukemia ◽  
Dependent Atpase ◽  
Myelocytic Leukemia ◽  
Dead Box ◽  
Double Stranded Dna ◽  
Atpase Assay ◽  
Sporadic Cases ◽  
Dna Translocase

The human DEAD (Asp–Glu–Ala–Asp) box protein DDX41, a member of the DEXDc helicase family, has nucleic acid–dependent ATPase and RNA and DNA translocase and unwinding activities. DDX41 is affected by somatic mutations in sporadic cases of myeloid neoplasms as well as in a biallelic fashion in 50% of patients with germline DDX41 mutations. The R525H mutation in DDX41 is thought to play important roles in the development of hereditary myelodysplastic syndrome and acute myelocytic leukemia. In this study, human DDX41 and its R525H mutant (R525H) were expressed in Escherichia coli and purified. The ATPase activities of the recombinant DDX41 and R525H proteins were dependent on both ATP and double-stranded DNA (dsDNA), such as poly(dG–dC) and poly(dA–dT). High-throughput screening was performed with a dsDNA-dependent ATPase assay using the human R525H proteins. After hit confirmation and counterscreening, several small-molecule inhibitors were successfully identified. These compounds show DDX41-selective inhibitory activities.

scholarly journals Replication Fork Slowing and Reversal upon DNA Damage Require PCNA Polyubiquitination and ZRANB3 DNA Translocase Activity

2017 ◽  
Vol 67 (5) ◽  
pp. 882-890.e5 ◽  
Author(s):  
Marko Vujanovic ◽  
Jana Krietsch ◽  
Maria Chiara Raso ◽  
Nastassja Terraneo ◽  
Ralph Zellweger ◽  
...  
Keyword(s):  
Dna Damage ◽  
Replication Fork ◽  
Dna Translocase

scholarly journals Contrasting Effects of σE on Compartmentalization of σF Activity during Sporulation of Bacillus subtilis

2004 ◽  
Vol 186 (7) ◽  
pp. 1983-1990 ◽  
Author(s):  
David W. Hilbert ◽  
Vasant K. Chary ◽  
Patrick J. Piggot
Keyword(s):  
Gene Expression ◽  
Transcription Factor ◽  
Bacillus Subtilis ◽  
Mother Cell ◽  
Cell Fates ◽  
Gene Encoding ◽  
Primitive Form ◽  
Small Proteins ◽  
Dna Translocase

ABSTRACT Spore formation by Bacillus subtilis is a primitive form of development. In response to nutrient starvation and high cell density, B. subtilis divides asymmetrically, resulting in two cells with different sizes and cell fates. Immediately after division, the transcription factor σF becomes active in the smaller prespore, which is followed by the activation of σE in the larger mother cell. In this report, we examine the role of the mother cell-specific transcription factor σE in maintaining the compartmentalization of gene expression during development. We have studied a strain with a deletion of the spoIIIE gene, encoding a DNA translocase, that exhibits uncompartmentalized σF activity. We have determined that the deletion of spoIIIE alone does not substantially impact compartmentalization, but in the spoIIIE mutant, the expression of putative peptidoglycan hydrolases under the control of σE in the mother cell destroys the integrity of the septum. As a consequence, small proteins can cross the septum, thereby abolishing compartmentalization. In addition, we have found that in a mutant with partially impaired control of σF, the activation of σE in the mother cell is important to prevent the activation of σF in this compartment. Therefore, the activity of σE can either maintain or abolish the compartmentalization of σF, depending upon the genetic makeup of the strain. We conclude that σE activity must be carefully regulated in order to maintain compartmentalization of gene expression during development.

scholarly journals Single-molecule imaging reveals mechanisms of protein disruption by a DNA translocase

Nature ◽  
2010 ◽  
Vol 468 (7326) ◽  
pp. 983-987 ◽  
Author(s):  
Ilya J. Finkelstein ◽  
Mari-Liis Visnapuu ◽  
Eric C. Greene
Keyword(s):  
Single Molecule ◽  
Single Molecule Imaging ◽  
Dna Translocase

scholarly journals Role of Double-Stranded DNA Translocase Activity of Human HLTF in Replication of Damaged DNA

2009 ◽  
Vol 30 (3) ◽  
pp. 684-693 ◽  
Author(s):  
András Blastyák ◽  
Ildikó Hajdú ◽  
Ildikó Unk ◽  
Lajos Haracska
Keyword(s):  
Translesion Synthesis ◽  
Dna Lesions ◽  
Template Switching ◽  
Replication Forks ◽  
Double Stranded Dna ◽  
Fork Regression ◽  
Dna Translocase ◽  
Damaged Dna

ABSTRACT Unrepaired DNA lesions can block the progression of the replication fork, leading to genomic instability and cancer in higher-order eukaryotes. In Saccharomyces cerevisiae, replication through DNA lesions can be mediated by translesion synthesis DNA polymerases, leading to error-free or error-prone damage bypass, or by Rad5-mediated template switching to the sister chromatid that is inherently error free. While translesion synthesis pathways are highly conserved from yeast to humans, very little is known of a Rad5-like pathway in human cells. Here we show that a human homologue of Rad5, HLTF, can facilitate fork regression and has a role in replication of damaged DNA. We found that HLTF is able to reverse model replication forks, a process which depends on its double-stranded DNA translocase activity. Furthermore, from analysis of isolated dually labeled chromosomal fibers, we demonstrate that in vivo, HLTF promotes the restart of replication forks blocked at DNA lesions. These findings suggest that HLTF can promote error-free replication of damaged DNA and support a role for HLTF in preventing mutagenesis and carcinogenesis, providing thereby for its potential tumor suppressor role.

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