A RGG motif protein is involved in Toxoplasma gondii stress-mediated response.

作者: Younes Boulila , Stanislas Tomavo , Mathieu Gissot

DOI: 10.1016/J.MOLBIOPARA.2014.07.009

关键词:

摘要: Abstract The molecular mechanisms controlling gene expression are still poorly understood in apicomplexan parasites. Here, we report the characterization of a homolog single strand binding proteins (named TgSsossB) Toxoplasma gondii. We previously showed that TgSsossB interacts with TgAlba involved translation regulation. examined role stress-mediated response, and particularly its rginine– g lycine– lycine (RGG) repeats domain. recombinant protein is able to bind DNA RNA sequence-independent manner, but not double stranded DNA. RGG motif this ability nucleic acid. produced mutant tagged strain lacking using knock-in strategy. observed exhibited fitness defect compared parental Moreover, fewer plaques stress conditions, due slow growth phenotype when extracellular parasites exposed stress. At level, lost interact TgAlba2 an isoform TgAlba1, indicating complex likely non-functional those Thus, our findings define domain as protein–protein interaction platform underline TgAlba–TgSsossB response.

参考文章(19)
Michael S. Behnke, John C. Wootton, Margaret M. Lehmann, Josh B. Radke, Olivier Lucas, Julie Nawas, L. David Sibley, Michael W. White, Coordinated Progression through Two Subtranscriptomes Underlies the Tachyzoite Cycle of Toxoplasma gondii PLoS ONE. ,vol. 5, pp. e12354- ,(2010) , 10.1371/JOURNAL.PONE.0012354
B. R. Joyce, S. F. Queener, R. C. Wek, W. J. Sullivan, Phosphorylation of eukaryotic initiation factor-2α promotes the extracellular survival of obligate intracellular parasite Toxoplasma gondii Proceedings of the National Academy of Sciences of the United States of America. ,vol. 107, pp. 17200- 17205 ,(2010) , 10.1073/PNAS.1007610107
Michael S. Behnke, Josh B. Radke, Aaron T. Smith, William J. Sullivan Jr, Michael W. White, The transcription of bradyzoite genes in Toxoplasma gondii is controlled by autonomous promoter elements. Molecular Microbiology. ,vol. 68, pp. 1502- 1518 ,(2008) , 10.1111/J.1365-2958.2008.06249.X
Jan Mani, Andreas Güttinger, Bernd Schimanski, Manfred Heller, Alvaro Acosta-Serrano, Pascale Pescher, Gerald Späth, Isabel Roditi, Alba-domain proteins of Trypanosoma brucei are cytoplasmic RNA-binding proteins that interact with the translation machinery. PLOS ONE. ,vol. 6, ,(2011) , 10.1371/JOURNAL.PONE.0022463
Arnaud Chêne, Shruthi S. Vembar, Loïc Rivière, José Juan Lopez-Rubio, Aurelie Claes, T. Nicolai Siegel, Hiroshi Sakamoto, Christine Scheidig-Benatar, Rosaura Hernandez-Rivas, Artur Scherf, PfAlbas constitute a new eukaryotic DNA/RNA-binding protein family in malaria parasites Nucleic Acids Research. ,vol. 40, pp. 3066- 3077 ,(2012) , 10.1093/NAR/GKR1215
Purusharth Rajyaguru, Roy Parker, RGG motif proteins: Modulators of mRNA functional states Cell Cycle. ,vol. 11, pp. 2594- 2599 ,(2012) , 10.4161/CC.20716
C. Cole, J. D. Barber, G. J. Barton, The Jpred 3 secondary structure prediction server Nucleic Acids Research. ,vol. 36, pp. 197- 201 ,(2008) , 10.1093/NAR/GKN238
Mathieu Gissot, Robert Walker, Stephane Delhaye, Tchilabalo Dilezitoko Alayi, Ludovic Huot, David Hot, Isabelle Callebaut, Christine Schaeffer-Reiss, Alain Van Dorsselaer, Stanislas Tomavo, Toxoplasma gondii Alba Proteins Are Involved in Translational Control of Gene Expression Journal of Molecular Biology. ,vol. 425, pp. 1287- 1301 ,(2013) , 10.1016/J.JMB.2013.01.039
Deborah M. Briercheck, Todd C. Wood, Timothy J. Allison, John P. Richardson, Gordon S. Rule, The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions. Nature Structural & Molecular Biology. ,vol. 5, pp. 393- 399 ,(1998) , 10.1038/NSB0598-393