RNA-DNA differences are generated in human cells within seconds after RNA exits polymerase II.
Published: Cell Reports 2014 Mar 13; 6(5):906-15. @...
NIH Research: March 2014
March 1, 2014
PLOS: November 2013
November 1, 2013
Protein Interaction Analysis of Senataxin and the ALS4 L389S Mutant Yields Insights into Senataxin Post-Translational Modification and Uncovers Mutant-Specific Binding with a Brain Cytoplasmic RNA-Encoded Peptide
Published: PLOS One, November 11, 2013, DOI: 10.1371/journal.pone.0078837
Authors: Craig L. Bennett, Y Chen, M Vignali, RS Lo, AG Mason, A Unal, NP Huq Saifee, S Fields, Albert R. La Spada.
Genetic mutations in senataxin lead to two neurological diseases, juvenile amyotrophic lateral sclerosis (ALS4) and ataxia ocular apraxia (AOA2). Proteins function in conjunction with other proteins. Interactions with protein partners are essential for maintaining proper cell functions. The proteins that senataxin interacts with are mostly unknown; and this information is important to inform us of its function. In this paper, Bennett and La Spada uncovered that senataxin with an ALS4 mutation interacts with proteins that are similar to a brain-specific RNA; however, senataxin without the ALS4 mutation does not interact with these proteins. This finding demonstrates that the ALS4-form of senataxin may have different binding partners than the normal protein, and these alternate partners may contribute to ALS4. Our senataxin protein interaction study reveals a number of features of senataxin biology that shed light on senataxin normal function and likely on senataxin molecular pathology in ALS4.