Understanding a multi-functional protein family: Exploring DBHS protein dynamics and function. — ASN Events
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  2. Session Ten - Poster Session C
  3. Understanding a multi-functional protein family: Exploring DBHS protein dynamics and function.

Understanding a multi-functional protein family: Exploring DBHS protein dynamics and function. (#312)

Gavin J. Knott 1 , Mihwa Lee 1 , Archa H. Fox 2 , Charles S. Bond 1
  1. University of Western Australia, Crawley, WA, Australia
  2. West Australian Institute of Medical Research, Perth, WA, Australia

The Drosophila behaviour/human splicing (DBHS) proteins are a family of obligatory dimeric proteins found in higher order mammals down to the simplest invertebrates. In humans, the family consists of three highly conserved members that exist combinatorially as homo- and heterodimeric complexes consistently implicated in a multitude of nuclear gene regulatory processes 1.

In mammals, DBHS proteins form the primary protein component of the ribonucleoprotein subnuclear complex, the paraspeckle 2. However, what factors effect where and when a DBHS protein carries out a specified nuclear activity? It is tempting to suggest that the DBHS dimer composition and higher order complex state dictates alternative RNA and protein interaction partners.

Here we report the first detailed analysis into DBHS dynamics, particularly their dimerisation propensities. In vitro exchange experiments suggest that DBHS proteins prefer a heterodimeric state, highlighting the need for a more robust assessment of in vivo DBHS function. Furthermore, it may be possible to explain these preferences for dimerisation based on the extensive interaction interface of the dimer 3. 

  1. Y. Shav-Tal and D. Zipori, Febs Letters, 531, 109 – 114, (2002)
  2. A. H. Fox and A. I. Lamond, Cold Spring Harbour Perspectives in Biology, 2, (2010)
  3. D. M. Passon and M. Lee et al, Proc Natl Acad Sci USA, 109, 4846 – 4850, (2012)