Linked Life Data

14969691

Source:http://linkedlifedata.com/resource/pubmed/id/14969691

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2004-2-18
pubmed:abstractText
The RNA binding protein RBP16 regulates mitochondrial RNA editing and stability in Trypanosoma brucei. To aid in understanding the biochemical mechanisms of RBP16 function, we analyzed the RNA and protein binding capacity of RBP16 and its individual cold shock (CSD) and RGG domains. Both recombinantly expressed domains possess RNA binding activity. However, the specificity and affinity of RBP16 for gRNA is mediated predominantly through the interaction of the CSD with poly(U). The RGG domain contributes to the association between full length RBP16 and gRNA, as it was required for maximal binding. We further demonstrate that both domains contribute to maximal binding of RBP16 to the mitochondrial p22 protein. However, p22 can interact with the CSD alone and stimulate its gRNA binding activity. Thus, the CSD is primary in RBP16 interactions, while the RGG domain enhances the capacity of the CSD to bind both RNA and protein. These results suggest a model for RBP16 molecular interactions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0014-4894
pubmed:author
pubmed:issnType
Print
pubmed:volume
105
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
140-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Trypanosoma brucei: functions of RBP16 cold shock and RGG domains in macromolecular interactions.
pubmed:affiliation
Department of Microbiology and Immunology and Witebsky Center for Microbial Pathogenesis and Immunology, SUNY Buffalo School of Medicine, Buffalo, NY, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.