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      The Chromatin Remodeling Factor SMARCB1 Forms a Complex with Human Cytomegalovirus Proteins UL114 and UL44

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          Abstract

          Background

          Human cytomegalovirus (HCMV) uracil DNA glycosylase, UL114, is required for efficient viral DNA replication. Presumably, UL114 functions as a structural partner to other factors of the DNA-replication machinery and not as a DNA repair protein. UL114 binds UL44 (HCMV processivity factor) and UL54 (HCMV-DNA-polymerase). In the present study we have searched for cellular partners of UL114.

          Methodology/Principal Findings

          In a yeast two-hybrid screen SMARCB1, a factor of the SWI/SNF chromatin remodeling complex, was found to be an interacting partner of UL114. This interaction was confirmed in vitro by co-immunoprecipitation and pull-down. Immunofluorescence microscopy revealed that SMARCB1 along with BRG-1, BAF170 and BAF155, which are the core SWI/SNF components required for efficient chromatin remodeling, were present in virus replication foci 24–48 hours post infection (hpi). Furthermore a direct interaction was also demonstrated for SMARCB1 and UL44.

          Conclusions/Significance

          The core SWI/SNF factors required for efficient chromatin remodeling are present in the HCMV replication foci throughout infection. The proteins UL44 and UL114 interact with SMARCB1 and may participate in the recruitment of the SWI/SNF complex to the chromatinized virus DNA. Thus, the presence of the SWI/SNF chromatin remodeling complex in replication foci and its association with UL114 and with UL44 might imply its involvement in different DNA transactions.

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          Most cited references58

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          The biology of chromatin remodeling complexes.

          The packaging of chromosomal DNA by nucleosomes condenses and organizes the genome, but occludes many regulatory DNA elements. However, this constraint also allows nucleosomes and other chromatin components to actively participate in the regulation of transcription, chromosome segregation, DNA replication, and DNA repair. To enable dynamic access to packaged DNA and to tailor nucleosome composition in chromosomal regions, cells have evolved a set of specialized chromatin remodeling complexes (remodelers). Remodelers use the energy of ATP hydrolysis to move, destabilize, eject, or restructure nucleosomes. Here, we address many aspects of remodeler biology: their targeting, mechanism, regulation, shared and unique properties, and specialization for particular biological processes. We also address roles for remodelers in development, cancer, and human syndromes.
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            Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits.

            Protein complexes of the SWI/SNF family remodel nucleosome structure in an ATP-dependent manner. Each complex contains between 8 and 15 subunits, several of which are highly conserved between yeast, Drosophila, and humans. We have reconstituted an ATP-dependent chromatin remodeling complex using a subset of conserved subunits. Unexpectedly, both BRG1 and hBRM, the ATPase subunits of human SWI/SNF complexes, are capable of remodeling mono-nucleosomes and nucleosomal arrays as purified proteins. The addition of INI1, BAF155, and BAF170 to BRG1 increases remodeling activity to a level comparable to that of the whole hSWI/SNF complex. These data define the functional core of the hSWI/SNF complex.
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              Cooperation between complexes that regulate chromatin structure and transcription.

              Chromatin structure creates barriers for each step in eukaryotic transcription. Here we discuss how the activities of two major classes of chromatin-modifying complexes, ATP-dependent remodeling complexes and HAT or HDAC complexes, might be coordinated to create a DNA template that is accessible to the general transcription apparatus.
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                Author and article information

                Contributors
                Role: Editor
                Journal
                PLoS One
                PLoS ONE
                plos
                plosone
                PLoS ONE
                Public Library of Science (San Francisco, USA )
                1932-6203
                2012
                27 March 2012
                : 7
                : 3
                : e34119
                Affiliations
                [1 ]Department of Microbiology, University of Oslo and Oslo University Hospital HF, Rikshospitalet, Oslo, Norway
                [2 ]Department of Medical Biochemistry, University of Oslo and Oslo University Hospital HF, Rikshospitalet, Oslo, Norway
                [3 ]Centre for Molecular Biology and Neuroscience, University of Oslo and Oslo University Hospital HF, Rikshospitalet, Oslo, Norway
                University of Sussex, United Kingdom
                Author notes

                Conceived and designed the experiments: TRN HR RS LL MB. Performed the experiments: TRN RS PHB LL ØO. Analyzed the data: TRN HR LL MB. Contributed reagents/materials/analysis tools: HR MB. Wrote the paper: TRN HR LL MB.

                Article
                PONE-D-11-17460
                10.1371/journal.pone.0034119
                3313996
                22479537
                61f02691-9a7e-4563-8bac-3dbb16b05901
                Ranneberg-Nilsen et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
                History
                : 7 September 2011
                : 22 February 2012
                Page count
                Pages: 12
                Categories
                Research Article
                Biology
                Biochemistry
                Nucleic Acids
                DNA
                Proteins
                Microbiology
                Virology
                Viral Replication
                Proteomics
                Medicine
                Infectious Diseases
                Viral Diseases

                Uncategorized
                Uncategorized

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