Linked Life Data

19309309

Source:http://linkedlifedata.com/resource/pubmed/id/19309309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-5-22
pubmed:abstractText
Actin, the major component of the cytoplasmic skeleton, has been shown to exist in the nucleus. Nuclear actin functions in several steps of the transcription process, including chromatin remodelling and transcription initiation and elongation. However, as a part of PICs (pre-initiation complexes), the role of actin remains to be elucidated. In the present study, we identified RHA (RNA helicase A) as an actin-interacting protein in PICs. Using immunoprecipitation and immunofluorescence techniques, we have shown that RHA associates with beta-actin in the nucleus. A GST (glutathione transferase) pulldown assay using different deletion mutants revealed that the RGG (Arg-Gly-Gly) region of RHA was responsible for the interaction with beta-actin, and this dominant-negative mutant reduced the recruitment of Pol II (RNA polymerase II) into PICs. Moreover, overexpression or depletion of RHA could influence the interaction of Pol II with beta-actin and beta-actin-involved gene transcription regulation. These results suggest that RHA acts as a bridging factor linking nuclear beta-actin with Pol II.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1470-8728
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
420
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
421-8
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
RNA helicase A acts as a bridging factor linking nuclear beta-actin with RNA polymerase II.
pubmed:affiliation
Institute of Genetics and Cytology, Northeast Normal University, Changchun, Jilin, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't