Insilico Analysis of a Rice SR Related Protein, SRCTD-6 Reveals a Splicing Function

Simmanna Nakka ^[2] | Uday Bhaskar Sajja ^[2]

Abstract: RS domain containing proteins are associated with binding to the exons of nascent primary transcript and recruiting components of spliceosome for precise recognition of the splice junctions. This is achieved with the help of RRM domain by which the protein binds with the RNA. However there are proteins which share the domain characteristics of SR proteins but lacking the RRMs. These proteins are grouped under SR related proteins. Here we described a SR Related CTD associate factor-6 (SRCTD-6) which contains unique set of domains. Insilco analysis of this protein identified a hydrophilic signature with coiled domains and 2 distinct helices. Domain characterization revealed the presence of an RPR domain, an RS domain in the C-terminal and stretches of Prolines and Glutamines in the N-terminus. Structural analysis of this protein hypothesise that it is recruited at the splice junction by Heptad repeats of C-terminal domain of RNA polymerase II. We predict that SRCTD-6 has a general role in identifying the precise 5I and 3I splice junctions.

Keywords: spliceosome, RPR-Domain, homology modelling, hydropathacity

Edition: Volume 10 Issue 11, November 2021,

Pages: 152 - 155