hNMP 200: A Novel Human Common Nuclear Matrix Protein Combining Structural and Regulatory Functions

Gotzmann, Josef; Gerner, Christopher; Meißner, Michael; Holzmann, Klaus; Grimm, Rudolf; Mikulits, Wolfgang; Sauermann, Georg

doi:10.1006/excr.2000.5025

Cited by 33 publications

(26 citation statements)

References 40 publications

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“…Of significance to understanding Prp19p function, we have found that Prp19p is required to maintain the organization of the Ntc unit, including Cef1p, Cwc2p, Snt309p, Prp46p, Syf1p, and Clf1p+ These data, coupled with the recent observation that hNMP200, a nuclear matrix protein, represents hPRP19 (Gotzmann et al+, 2000) suggests a role for Prp19p as a scaffolding protein+ In this scenario, Prp19p, which is believed to have the ability to oligomerize (Cheng et al+, 1993), would provide a platform for Cef1p, Snt309p, Cwc2p, and other components of the Ntc complex to organize upon+ That proteins other than those described here bind Prp19p directly is likely, as no protein interactions have yet been mapped to its U-box or WD40 repeats+…”

Section: Discussionmentioning

confidence: 81%

Characterization of interactions among the Cef1p-Prp19p-associated splicing complex

Ohi

Gould

2002

RNA

104

146

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Section: Discussionmentioning

confidence: 81%

Characterization of interactions among the Cef1p-Prp19p-associated splicing complex

Ohi

Gould

2002

RNA

104

146

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“…Previous studies have shown that the Pso4 complex has a defined and conserved role in pre-mRNA splicing (25-29, 62, 63) and has been implicated in the repair of damaged DNA in both yeast and mammalian cells (24,25,32). Furthermore, at least one member of this complex, Pso4/Prp19, has been shown in mammalian cells to fractionate with the nuclear matrix (31). In particular, this latter observation may suggest a plausible mechanism by which the Pso4 complex might participate in both pre-mRNA splicing reactions and DNA damage processing.…”

Section: Discussionmentioning

confidence: 93%

“…Thus, PRP19/PSO4 appears to play dual roles in the cell; it has an essential function in pre-mRNA splicing and a role in the processing of DNA lesions particularly ICLs. Interestingly, human Pso4/Prp19 has also been isolated from human cell extracts as a component of the nuclear matrix and termed NMP200 (31). The human protein has also been shown to interact with terminal deoxynucleotidyltransferase and to be involved in mediating cell survival after DNA damage (32).…”

mentioning

confidence: 99%

The Pso4 mRNA Splicing and DNA Repair Complex Interacts with WRN for Processing of DNA Interstrand Cross-links

Zhang

Kaur

et al. 2005

Journal of Biological Chemistry

110

116

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DNA interstrand cross-links (ICLs) are perhaps the most formidable lesion encountered by the cellular DNA repair machinery, and the elucidation of the process by which they are removed in eukaryotic cells has proved a daunting task. In particular, the early stages of adduct recognition and uncoupling of the cross-link have remained elusive principally because genetic studies have not been highly revealing. We have developed a biochemical assay in which processing of a DNA substrate containing a site-specific psoralen ICL can be monitored in vitro. Using this assay we have shown previously that the mismatch repair factor MutS␤, the nucleotide excision repair heterodimer Ercc1-Xpf, and the replication proteins RPA and PCNA are involved in an early stage of psoralen ICL processing. Here, we report the identification of two additional factors required in the ICL repair process, a previously characterized pre-mRNA splicing complex composed of Pso4/Prp19, Cdc5L, Plrg1, and Spf27 (Pso4 complex), and WRN the protein deficient in Werner syndrome. Analysis of the WRN protein indicates that its DNA helicase function, but not its exonuclease activity, is required for ICL processing in vitro. In addition, we show that WRN and the Pso4 complex interact through a direct physical association between WRN and Cdc5L. A putative model for uncoupling of ICLs in mammalian cells is presented.

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“…9 HeLa cells expressing a hNMP 200-GFP fusion protein were induced to undergo apoptosis by treatment with 2.5 mM staurosporine. In untreated cells colocalization of hNMP 200 and chromatin, except in nucleolar regions, was evident ( Figure 1E,F).…”

Section: Resultsmentioning

confidence: 99%

Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation

et al. 2002

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The nuclear matrix (NM) is considered a proteinaceous scaffold spatially organizing the interphase nucleus, the integrity of which is affected during apoptosis. Caspasemediated degradation of NM proteins, such as nuclear lamins, precedes apoptotic chromatin condensation (ACC). Nevertheless, other NM proteins remain unaffected, which most likely maintain a remaining nuclear structure devoid of chromatin. We, therefore, screened various types of apoptotic cells for changes of the nuclear matrix proteome during the process of apoptotic ACC. Expectedly, we observed fundamental alterations of known chromatin-associated proteins, comprising both degradation and translocation to the cytosol. Importantly, a consistent set of abundant NM proteins, some (e.g. hNMP 200) of which displaying structural features, remained unaffected during apoptosis and might therefore represent constituents of an elementary scaffold. In addition, proteins involved in DNA replication and DNA repair were found accumulated in the NM fraction before cells became irreversibly committed to ACC, a time point characterized in detail by inhibitor studies with orthovanadate. In general, protein alterations of a consistent set of NM proteins (67 of which were identified), were reproducibly detectable in Fasinduced Jurkat cells, in UV-light treated U937 cells and also in staurosporine-treated HeLa cells. Our data indicate that substantial alterations of proteins linking chromatin to an elementary nuclear protein scaffold might play an intriguing role for the process of ACC.

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hNMP 200: A Novel Human Common Nuclear Matrix Protein Combining Structural and Regulatory Functions

Cited by 33 publications

References 40 publications

Characterization of interactions among the Cef1p-Prp19p-associated splicing complex

Characterization of interactions among the Cef1p-Prp19p-associated splicing complex

The Pso4 mRNA Splicing and DNA Repair Complex Interacts with WRN for Processing of DNA Interstrand Cross-links

Proteome analysis of nuclear matrix proteins during apoptotic chromatin condensation

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