Linked Life Data

21637296

Source:http://linkedlifedata.com/resource/pubmed/id/21637296

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2011-7-1
pubmed:abstractText
Single-molecule techniques have been used for only a subset of biological problems because of difficulties in studying proteins that require cofactors or post-translational modifications. Here, we present a new method integrating single-molecule fluorescence microscopy and immunopurification to study protein complexes. We used this method to investigate Lin28-mediated microRNA uridylation by TUT4 (terminal uridylyl transferase 4, polyU polymerase), which regulates let-7 microRNA biogenesis. Our real-time analysis of the uridylation by the TUT4 immunoprecipitates suggests that Lin28 functions as a processivity factor of TUT4. Our new technique, SIMPlex (single-molecule approach to immunoprecipitated protein complexes), provides a universal tool to analyse complex proteins at the single-molecule level.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1469-3178
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
690-6
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Single-molecule approach to immunoprecipitated protein complexes: insights into miRNA uridylation.
pubmed:affiliation
School of Biological Sciences and Creative Research Center, Seoul National University, Seoul 151-742, Korea; Kavli Institute of NanoScience and Department of BioNanoScience, Delft University of Technology, Lorentzweg 1, Delft 2628 CJ, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't