Abstract
RNA-binding proteins (RBPs) have important functions in the regulation of gene expression. RBPs play key roles in post-transcriptional processes in all eukaryotes, such as splicing regulation, mRNA transport and modulation of mRNA translation and decay. RBPs assemble into different mRNA-protein complexes, which form messenger ribonucleoprotein complexes (mRNPs). Gene expression regulation in trypanosomatids occurs mainly at the post-transcriptional level and RBPs play a key role in all processes. However, the functional characterization of RBPs in Trypanosoma cruzi has been impaired due to the lack of reliable reverse genetic manipulation tools. The comparison of RBPs from Saccharomyces cerevisiae and T. cruzi might allow inferring on the function of these proteins based on the information available for the orthologous RNA-binding proteins from the S. cerevisiae model organism. In this review, we discuss the role of some RBPs from T. cruzi and their homologues in regulating gene expression in yeast.
Highlights
Gene expression involves several events that occur at the transcriptional and post-transcriptional levels
RNA-binding proteins (RBPs) assemble into different mRNA-protein complexes, which form messenger ribonucleoprotein complexes
Gene expression regulation in trypanosomatids occurs mainly at the post-transcriptional level and RBPs play a key role in all processes
Summary
Gene expression involves several events that occur at the transcriptional and post-transcriptional levels. Eukaryotic type I and prokaryotic type II KH domains share a minimal baab core, with two additional a and b elements positioned either in C-terminal (type I, eukaryotes) or N-terminal (type II, prokaryotes) orientation to this core motif (Grishin, 2001) This structure directs four nucleic acid bases towards a groove inside the protein structure where hydrophobic interactions and a network of main chain and side chain hydrogen bonds mediate nucleobase recognition. The C2H2 class of zinc finger protein has been shown to bind preferentially to RNA targets These zinc fingers are characterized by three cysteine residues and one histidine residue that coordinate the zinc ion and form the Cys-X7-8-Cys-X5-Cys-X3-His sequence (Hall, 2005). The dsRBD is a conserved protein domain of approximately 65–70 amino acids which binds to double-stranded or highly structured RNAs (Finn et al, 2010). MRNA processing/stability Regulator of a specific subset of mRNAs mRNA destabilizing factor mRNA destabilizing factor mRNA destabilizing factor Involved in differentiation Involved in differentiation Involved in differentiation, translation regulator Regulator of a specific subset of mRNAs Involved in differentiation Involved regulation of splicing
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.