Abstract：
:The heterogeneous nuclear ribonucleoprotein K protein is an RNA-binding protein found in several subcellular compartments where it is thought to be involved in signaling multiple processes that compose gene expression. K protein contains three K homology (KH) domains that mediate RNA-binding. We used a serial analysis of gene expression (SAGE)-based strategy, yeast three-hybrid screen, RNA pull-down assays and computational analysis to characterize K protein-associated RNAs. We demonstrate that K protein interacts with many sense and antisense nuclear and mitochondrial transcripts through both direct and indirect binding. The highly specific direct binding of transcripts to K protein is mediated by a consensus sequence comprising three C-rich patches. Structural analysis suggests a three-prong interaction model whereby each of the three KH domains binds one of the C-rich patches. Genome-wide and yeast three-hybrid clone analysis revealed that these sequences are located preferentially in the 3' untranslated regions, which are known to regulate mRNA translation and processing.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Klimek-Tomczak K,Wyrwicz LS,Jain S,Bomsztyk K,Ostrowski Jdoi
10.1016/j.jmb.2004.07.099keywords:
subject
Has Abstractpub_date
2004-09-24 00:00:00pages
1131-41issue
4eissn
0022-2836issn
1089-8638pii
S0022-2836(04)00953-2journal_volume
342pub_type
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