Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2

Mertens, C., Hofmann, I., Wang, Z. X., Teichmann, M., Chong, S. S., Schnolzer, M., Franke, W. W. (July 2001) Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2. Proceedings of the National Academy of Sciences of the United States of America, 98 (14). pp. 7795-7800. ISSN 0027-8424

[thumbnail of Sepedheri_PNAS_2001.pdf]
Preview
PDF
Sepedheri_PNAS_2001.pdf - Published Version

Download (558kB) | Preview
URL: http://www.ncbi.nlm.nih.gov/pubmed/11416169
DOI: 10.1073/pnas.141219498

Abstract

Plakophilin 2, a member of the arm-repeat protein family, is a dual location protein that occurs both in the cytoplasmic plaques of desmosomes as an architectural component and in an extractable form in the nucleoplasm. Here we report the existence of two nuclear particles containing plakophilin 2 and the largest subunit of RNA polymerase (pol) III (RPC155), both of which colocalize and are coimmuno-selected with other pol III subunits and with the transcription factor TFIIIB, We also show that plakophilin 2 is present in the pol III holoenzyme. but not the core complex, and that it binds specifically to RPC155 in vitro. We propose the existence of diverse nuclear particles in which proteins known as plaque proteins of intercellular junctions are complexed with specific nuclear proteins.

Item Type: Paper
Uncontrolled Keywords: TRANSCRIPTION FACTOR LEF-1 BETA-CATENIN DESMOSOMAL PLAQUE EUKARYOTIC TRANSCRIPTION BINDING-PROTEIN XENOPUS EMBRYOS LARGEST SUBUNIT BAND-6 PROTEIN COILED BODIES CAJAL BODIES
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > RNA polymerase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > nuclear ribonucleoprotein
CSHL Authors:
Communities: CSHL labs > Hernandez lab
Depositing User: Matt Covey
Date: July 2001
Date Deposited: 17 Jan 2014 19:59
Last Modified: 10 Sep 2019 19:10
PMCID: PMC35421
Related URLs:
URI: https://repository.cshl.edu/id/eprint/29272

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving