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PLoS One. 2012;7(1):e30029. doi: 10.1371/journal.pone.0030029. Epub 2012 Jan 12.

Characterization of a novel association between two trypanosome-specific proteins and 5S rRNA.

Author information

1
Department of Microbiology and Immunology & Witebsky Center for Microbial Pathogenesis and Immunology, University at Buffalo, Buffalo, New York, United States of America.

Abstract

P34 and P37 are two previously identified RNA binding proteins in the flagellate protozoan Trypanosoma brucei. RNA interference studies have determined that the proteins are essential and are involved in ribosome biogenesis. Here, we show that these proteins interact in vitro with the 5S rRNA with nearly identical binding characteristics in the absence of other cellular factors. The T. brucei 5S rRNA has a complex secondary structure and presents four accessible loops (A to D) for interactions with RNA-binding proteins. In other eukaryotes, loop C is bound by the L5 ribosomal protein and loop A mainly by TFIIIA. The binding of P34 and P37 to T. brucei 5S rRNA involves the LoopA region of the RNA, but these proteins also protect the L5 binding site located on LoopC.

PMID:
22253864
PMCID:
PMC3257258
DOI:
10.1371/journal.pone.0030029
[Indexed for MEDLINE]
Free PMC Article

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