Erratum

Tomita, Hiroyuki; Soshi, Takayuki; Inoue, Hirokazu

doi:10.1007/bf00283430

Cited by 3 publications

(5 citation statements)

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“…Targeting of two genes, mtr and ad-3A, on chromosomes IV and I, respectively, was conducted in these strains by a PCR-based method (16). In this study, exogenous DNA was introduced by electroporation (17,18), which is more efficient and convenient than the spheroplastpolyethylene glycol (PEG) method (19,20) used previously for transformation of Neurospora.…”

Section: Highly Efficient Gene Replacements In Neurospora Strains Defmentioning

confidence: 99%

Highly efficient gene replacements in Neurospora strains deficient for nonhomologous end-joining

Ninomiya

Suzuki

Ishii

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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541

453

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Gene disruption and overexpression play central roles in the analysis of gene function. Homologous recombination is, in principle, the most efficient method of disrupting, modifying, or replacing a target gene. Although homologous integration of exogenous DNA into the genome occurs readily in Saccharomyces cerevisiae , it is rare in many other organisms. We identified and disrupted Neurospora crassa genes homologous to human KU70 and KU80 , which encode proteins that function in nonhomologous end-joining of double-stranded DNA breaks. The resulting mutants, named mus - 51 and mus - 52 , showed higher sensitivity to methyl methanesulfonate, ethyl methanesulfonate, and bleomycin than wild type, but not to UV, 4-nitroquinoline 1-oxide, camptothecin, or hydroxyurea. Vegetative growth, conidiation, and ascospore production in homozygous crosses were normal. The frequency of integration of exogenous DNA into homologous sequences of the genome in the KU disruption strains of N. crassa was compared with that in wild type, mei-3 , and mus - 11 . In mei-3 and mus - 11 , which are defective in homologous recombination, none or few homologous integration events were observed under any conditions. When mtr target DNA with ≈2-kb 5′ and 3′ flanking regions was used for transformation of the KU disruption strains, 100% of transformants exhibited integration at the homologous site, compared to 10 to 30% for a wild-type recipient. Similar results were obtained when the ad-3A gene was targeted for disruption. These results indicate that KU disruption strains are efficient recipients for gene targeting.

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Section: Highly Efficient Gene Replacements In Neurospora Strains Defmentioning

confidence: 99%

Highly efficient gene replacements in Neurospora strains deficient for nonhomologous end-joining

Ninomiya

Suzuki

Ishii

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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541

453

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“…1B). However, hRAD18 and uvs-2 do not have the nucleotide-binding motif that is found in yeast RAD18 (7,8). Despite the high similarity between RAD18 and uvs-2, the uvs-2 gene cannot complement yeast rad18 mutant (7,8).…”

Section: Resultsmentioning

confidence: 96%

“…A homologue of RAD18 has been identified from the filamentous fungus Neurospora crassa. This gene, uvs-2, encodes a protein that shares 25.5% amino acid identity with Rad18 and interacts with a Rad6 homologue, MUS8 (7,8). In contrast to the yeast rad18 mutant, the uvs-2 mutant shows high mutation frequencies under both spontaneous and induced conditions (9)(10)(11).…”

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confidence: 99%

Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens

Tateishi

Sakuraba

Masuyama

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

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133

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Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. The yeast Saccharomyces cerevisiae Rad18 protein plays a pivotal role in the process together with the Rad6 protein. Here, we have cloned a human homologue of RAD18, hRAD18. It maps on chromosome 3p24 -25, where deletions are often found in lung, breast, ovary, and testis cancers. In vivo, hRad18 protein binds to hHR6 protein through a conserved ring-finger motif. Stable transformants with hRad18 mutated in this motif become sensitive to UV, methyl methanesulfonate, and mitomycin C, and are defective in the replication of UV-damaged DNA. Thus, hRAD18 is a functional homologue of RAD18.

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“…[16][17][18][19][20] The rad18 mutants of lower eukaryotic cells show hypersensitivity to DNA damaging agents such as ultraviolet (UV), methyl methanesulfonate (MMS), and mytomycin C (MMC). [21][22][23] In the case of higher eukaryotic cells, RAD18 Ϫ/Ϫ mouse embryonic stem cells and RAD18 Ϫ/Ϫ DT40 cells also show hypersensitivity to various DNA damaging agents such as UV and MMS. Moreover, both spontaneous and DNA damage-induced sister chromatid exchange (SCE) are elevated in RAD18 knockout vertebrate cells.…”

Section: Wrnip1mentioning

confidence: 99%

“…[16][17][18][19][20] The rad18 mutants of lower eukaryotic cells show hypersensitivity to DNA damaging agents such as ultraviolet (UV), methyl methanesulfonate (MMS), and mytomycin C (MMC). [21][22][23] Key words Rad18; WRN interacting protein 1 (WRNIP1); DT40; maintenance of genome stability 1 (Mgs1); RecQ; proliferating cell nuclear antigen (PCNA) …”

mentioning

confidence: 99%

Functional Relationships between Rad18 and WRNIP1 in Vertebrate Cells

Yoshimura

Seki

Hayashi

et al. 2006

Biological & Pharmaceutical Bulletin

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Werner syndrome (WS) is a rare autosomal recessive disorder characterized by premature aging associated with an early onset of age-related diseases, including arteriosclerosis, malignant neoplasms, melituria, and cataracts.1) The gene responsible for WS encodes WRN, a member of the RecQ family of DNA helicases.2) The protein possesses DNA helicase and exonuclease activities. [3][4][5][6] Accumulating evidence suggests that WRN has roles relevant to telomere function since it efficiently prevents telomere degradation and consequent genomic instability. 7,8) Other functions of WRN are not well understood, although additional roles in many aspects of cellular metabolism may be inferred by its physical interaction with proteins involved in DNA replication, repair, and recombination, including DNA polymerase d. 9)To obtain further insights into the function of WRN, we searched for WRN-interacting proteins by a two-hybrid strategy and found a novel protein which we initially denoted WHIP (Werner helicase interacting protein) 10) but which is now called WRNIP1 according to the nomenclatural conventions of HUGO. Interaction between the two proteins was further confirmed by their co-immunoprecipitation from cell extracts.The amino acid sequence of WRNIP1 is similar to that of replication factor C (RFC), and it also contains the Walker A and B motifs for ATP binding and/or ATPase activity.10) A homologue of WRNIP1, MGS1, has been identified in budding yeast.11) Previous studies have shown that overproduction of Mgs1 is lethal in mutants defective in proteins related to DNA replication, such as DNA polymerase d, RFC, PCNA, and RPA.12,13) Moreover, we showed that mutation of mgs1 partially alleviates the growth defect of the pol31 mutant, which bears a mutation in the second subunit of DNA polymerase d.13) Consequently, we proposed that Mgs1 (yWRNIP1) interacts with the DNA synthesis machinery to modulate the function of DNA polymerase d during replication or replication-associated repair.13) Indeed, we demonstrated that human WRNIP1 interacts with three of the four subunits of human DNA polymerase d and stimulates its activity. 14)To investigate the function of WRNIP1 in higher eukaryotic cells, we previously generated WRNIP1 gene knockout cells from chicken DT40 cells.15) Because the WRNIP1 gene resides on chromosome 2, which is trisomic in DT40 cells, all three alleles were disrupted by gene targeting. WRNIP1Ϫ/Ϫ/Ϫ cells showed a slight elevation of sister chromatid exchange (SCE) and moderate sensitivity to the anticancer drug camptothecin (CPT), 15) an inhibitor of DNA topoisomerase I (Top1), which forms a complex with DNA.It has been reported that the mgs1 (wrnip1) rad18 double mutation confers synthetic lethality in the budding yeast Saccharomyces cerevisiae.12) The yeast Rad18 protein is known to function in post-replication repair pathways, including an error-free damage bypass pathway involving Rad30 (Polh) and an error-prone damage bypass pathway involving Rev3/7 (Polz ). [16][17][18][19][20] The rad18 mutants of ...

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Erratum

Cited by 3 publications

References 0 publications

Highly efficient gene replacements in Neurospora strains deficient for nonhomologous end-joining

Highly efficient gene replacements in Neurospora strains deficient for nonhomologous end-joining

Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens

Functional Relationships between Rad18 and WRNIP1 in Vertebrate Cells

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