Identification in the rat brain of a set of nuclear proteins interacting with H1 degrees mRNA.

Authors: Di Liegro, CM  Schiera, G  Proia, P  Saladino, P  Di Liegro, I 
Citation: Di Liegro CM, etal., Neuroscience. 2013 Jan 15;229:71-6. doi: 10.1016/j.neuroscience.2012.10.072. Epub 2012 Nov 14.
Pubmed: (View Article at PubMed) PMID:23159318
DOI: Full-text: DOI:10.1016/j.neuroscience.2012.10.072

Synthesis of H1 degrees histone, in the developing rat brain, is also regulated at post-transcriptional level. Regulation of RNA metabolism depends on a series of RNA-binding proteins (RBPs); therefore, we searched for H1 degrees mRNA-interacting proteins. With this aim, we used in vitro transcribed, biotinylated H1 degrees RNA as bait to isolate, by a chromatographic approach, proteins which interact with this mRNA, in the nuclei of brain cells. Abundant RBPs, such as heterogeneous nuclear ribonucleoprotein (hnRNP) K and hnRNP A1, and molecular chaperones (heat shock cognate 70, Hsc70) were identified by mass spectrometry. Western blot analysis also revealed the presence of cold shock domain-containing protein 2 (CSD-C2, also known as PIPPin), a brain-enriched RBP previously described in our laboratory. Co-immunoprecipitation assays were performed to investigate the possibility that identified proteins interact with each other and with other nuclear proteins. We found that hnRNP K interacts with both hnRNP A1 and Hsc70 whereas there is no interaction between hnRNP A1 and Hsc70. Moreover, CSD-C2 interacts with hnRNP A1, Y box-binding protein 1 (YB-1), and hnRNP K. We also have indications that CSD-C2 interacts with Hsc70. Overall, we have contributed to the molecular characterization of a ribonucleoprotein particle possibly controlling H1 degrees histone expression in the brain.

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CRRD Object Information
CRRD ID: 10040996
Created: 2015-05-07
Species: All species
Last Modified: 2015-05-07
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.