Linked Life Data

20176811

Source:http://linkedlifedata.com/resource/pubmed/id/20176811

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2010-4-8
pubmed:abstractText
Protein complexes containing Prp19 play a central role during catalytic activation of the spliceosome, and Prp19 and its related proteins are major components of the spliceosome's catalytic core RNP. To learn more about the spatial organization of the human Prp19 (hPrp19)/CDC5L complex, which is comprised of hPrp19, CDC5L, PRL1, AD002, SPF27, CTNNBL1, and HSP73, we purified native hPrp19/CDC5L complexes from HeLa cells stably expressing FLAG-tagged AD002 or SPF27. Stoichiometric analyses indicated that, like Saccharomyces cerevisiae NTC (nineteen complex), the human Prp19/CDC5L complex contains four copies of hPrp19. Salt treatment identified a stable core comprised of CDC5L, hPrp19, PRL1, and SPF27. Protein-protein interaction studies revealed that SPF27 directly interacts with each component of the hPrp19/CDC5L complex core and also elucidated several additional, previously unknown interactions between hPrp19/CDC5L complex components. Limited proteolysis of the hPrp19/CDC5L complex revealed a protease-resistant complex comprised of SPF27, the C terminus of CDC5L, and the N termini of PRL1 and hPrp19. Under the electron microscope, purified hPrp19/CDC5L complexes exhibit an elongated, asymmetric shape with a maximum dimension of approximately 20 nm. Our findings not only elucidate the molecular organization of the hPrp19/CDC5L complex but also provide insights into potential protein-protein interactions at the core of the catalytically active spliceosome.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1098-5549
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2105-19
pubmed:dateRevised
2010-11-2
pubmed:meshHeading
pubmed-meshheading:20176811-Blotting, Far-Western, pubmed-meshheading:20176811-Cell Cycle Proteins, pubmed-meshheading:20176811-Chromatography, Affinity, pubmed-meshheading:20176811-Cross-Linking Reagents, pubmed-meshheading:20176811-HeLa Cells, pubmed-meshheading:20176811-Humans, pubmed-meshheading:20176811-Immunoprecipitation, pubmed-meshheading:20176811-Models, Biological, pubmed-meshheading:20176811-Multiprotein Complexes, pubmed-meshheading:20176811-Protein Binding, pubmed-meshheading:20176811-Protein Biosynthesis, pubmed-meshheading:20176811-Protein Processing, Post-Translational, pubmed-meshheading:20176811-Protein Stability, pubmed-meshheading:20176811-Protein Structure, Quaternary, pubmed-meshheading:20176811-Protein Structure, Tertiary, pubmed-meshheading:20176811-RNA-Binding Proteins, pubmed-meshheading:20176811-Salts
pubmed:year
2010
pubmed:articleTitle
Molecular architecture of the human Prp19/CDC5L complex.
pubmed:affiliation
Department of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, D-37077 Göttingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't