A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein

Takao, Masashi; Abramić, Marija; Moos, Malcolm; Otrin, Vesna Rapić; Wootton, John C.; McLenigan, Mary P.; Levine, Arthur S.; Protić, Miroslava

doi:10.1093/nar/21.17.4111

Cited by 99 publications

(72 citation statements)

References 44 publications

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“…Although UVDDB is suspected to play a role in nucleotide excision repair (NER) (Takao et al, 1993), we could not reveal an impact of X expression on this cellular function (Bergametti et al, 1999). Furthermore, despite extensive attempts, we found no qualitative or quantitative e ect of X protein on UVDDB-binding to UV-irradiated DNA, even with the class 1 WHx mutant (data not shown).…”

Section: Potential Role Of X-uvddb Interactionmentioning

confidence: 68%

“…In particular, UVDDB-HBx interaction is strongly a ected by mutations known to abolish HBx-mediated transactivation and human UVDDB also interacts with WHx and GSHx proteins (Sitterlin et al, 1997). However, there was no further clue for the biological relevance of UVDDB-X interaction, since no function has been proposed for UVDDB, besides a still elusive role in nucleotide excision repair (Hwang and Chu, 1993;Takao et al, 1993). In the present study, we designed a genetic screen to isolate WHx substitution mutants with signi®cantly altered UVDDB-binding.…”

Section: Introductionmentioning

confidence: 99%

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UVDDB p127-binding modulates activities and intracellular distribution of Hepatitis B virus X protein

2000

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Mammalian hepatitis B viruses encode a unique regulatory protein termed X, which is essential for infection and likely plays a role in the carcinogenic process associated with hepadnaviral infection. Among the numerous properties ascribed to X protein, two have been widely documented: promiscuous transcriptional transactivation and proapoptosis. However, full understanding of the mechanisms underlying these activities requires the identi®cation of the genuine X partners among the multiple X-binding host proteins. Here we show that (i) mutations in X protein, which markedly alter a nity for the host protein UVDDBp127, inactivate both transactivation and proapoptosis; (ii) ectopic fusion of a functional UVDDB-binding domain to a de®cient binding X mutant restored its activity; (iii) in contrast to the loss-of-binding mutants, a mutant with a strong gain-of-binding exerted trans-dominant negative e ects on wt X activity and localized in the nucleus and (iv) increase in intracellular UVDDB concentration enhanced both wt X-mediated transactivation and apoptosis. Taken together, our data provide strong evidence for a common upstream step in X mode of action, consisting of its productive interaction with UVDDB, via a structurally and functionally autonomous module. In addition, they underscore a nuclear location step of the viral protein that depends on its ability to bind UVDDB. Oncogene (2000) 19, 4417 ± 4426.

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Section: Potential Role Of X-uvddb Interactionmentioning

confidence: 68%

Section: Introductionmentioning

confidence: 99%

UVDDB p127-binding modulates activities and intracellular distribution of Hepatitis B virus X protein

2000

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“…Sequence analysis of this region predicts that it contains five β-propeller repeats [93]. This region of the sequence is highly similar to the spliceosomal U2 snRNP (human SAP130, yeast Rse1p) [94] and the UV damage recognition protein Xeroderma pigmentosum group E (XPE) [95]. A total of sixteen β-propeller repeats were identified in human CPSF-160 based on sequence analysis [96].…”

Section: Cpsf-160 (Cft1p/yhh1p)mentioning

confidence: 99%

Protein factors in pre-mRNA 3′-end processing

Mandel

Bai

Tong

2007

Cell. Mol. Life Sci.

364

482

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Most eukaryotic mRNA precursors (pre-mRNAs) must undergo extensive processing, including cleavage and polyadenylation at the 3′-end. Processing at the 3′-end is controlled by sequence elements in the pre-mRNA (cis elements) as well as protein factors. Despite the seeming biochemical simplicity of the processing reactions, more than 14 proteins have been identified for the mammalian complex, and more than 20 proteins have been identified for the yeast complex. The 3′-end processing machinery also has important roles in transcription and splicing. The mammalian machinery contains several sub-complexes, including cleavage and polyadenylation specificity factor (CPSF), cleavage stimulation factor (CstF), cleavage factor I (CF I m ), and cleavage factor II (CF II m ). Additional protein factors include poly(A) polymerase (PAP), poly(A) binding protein (PABP), symplekin, and the C-terminal domain (CTD) of RNA polymerase II largest subunit. The yeast machinery includes cleavage factor IA (CF IA), cleavage factor IB (CF IB), and cleavage and polyadenylation factor (CPF).

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“…XPC can be identified in S. cerevisiae, C. elegans and Drosophila. XPE, however, could only be clearly identified in C. elegans and not at present in Drosophila or S. cerevisiae, but has been reported in slime mold [19].…”

Section: Do We Know All Possible Strategies For Ner In All Organisms?mentioning

confidence: 83%

Nucleotide excision repair “a legacy of creativity”

Cleaver

Karplus

Kashani‐Sabet

et al. 2001

Mutation Research/DNA Repair

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The first half of the 20th century has seen an enormous growth in our knowledge of DNA repair, in no small part due to the work of Dirk Bootsma, Philip Hanawalt and Bryn Bridges; those honored by this issue. For the new millennium, we have asked three general questions: (A) Do we know all possible strategies of nucleotide excision repair (NER) in all organisms? (B) How is NER integrated and regulated in cells and tissues? (C) Does DNA replication represent a new frontier in the roles of DNA repair? We make some suggestions for the kinds of answers the next generation may provide. The kingdom of archea represents an untapped field for investigation of DNA repair in organisms with extreme lifestyles. NER appears to involve a similar strategy to the other kingdoms of prokaryotes and eukaryotes, but subtle differences suggest that individual components of the system may differ. NER appears to be regulated by several major factors, especially p53 and Rb which interact with transcription coupled repair and global genomic repair, respectively. Examples can be found of major regulatory changes in repair in testicular tissue and melanoma cells. Our understanding of replication of damaged DNA has undergone a revolution in recent years, with the discovery of multiple low-fidelity DNA polymerases that facilitate replicative bypass. A secondary mechanism of replication in the absence of NER or of one or more of these polymerases involves sister chromatid exchange and recombination (hMre11/hRad50/Nbs1). The relative importance of bypass and recombination is determined by the action of p53. We hypothesise that these polymerases may be involved in resolution of complex DNA structures during completion of replication and sister chromatid resolution. With these fascinating problems to investigate, the field of DNA repair will surely not disappoint the next generation.

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A 127 kDa component of a UV-damaged DNA-binding complex, which is defective in some xeroderma pigmentosum group E patients, is homologous to a slime mold protein

Cited by 99 publications

References 44 publications

UVDDB p127-binding modulates activities and intracellular distribution of Hepatitis B virus X protein

UVDDB p127-binding modulates activities and intracellular distribution of Hepatitis B virus X protein

Protein factors in pre-mRNA 3′-end processing

Nucleotide excision repair “a legacy of creativity”

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