What's new for 'Trypanosomatids' in PubMed

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Sent on Friday, 2010 Apr 16
Search kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
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PubMed Results

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1.	J Clin Microbiol. 2010 Apr 14. [Epub ahead of print] Rapid Identification of Old World Leishmaniasis by High Resolution Melting Analysis of the 7SL RNA gene. Nasereddin A, Jaffe CL. Department of Microbiology and Molecular Genetics, The Kuvin Center for the Study of Infectious and Tropical Diseases, IMRIC, Hebrew University-Hadassah Medical School, P. O. Box 12272, Jerusalem 91120 Israel. Abstract High resolution melt analysis polymerase chain reaction (HRM PCR) for diagnosis of Old World Leishmania was developed using the 7SL RNA gene. Cutaneous leishmaniasis samples were analyzed. Sensitivity and specificity of HRM PCR was significantly better (p<0.001) than the Internal Transcribed Spacer 1 PCR, and similar to kinetoplast DNA PCR.
	PMID: 20392923 [PubMed - as supplied by publisher]
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2.	J Biol Chem. 2010 Apr 14. [Epub ahead of print] Structure of the T. brucei p22 protein, a cytochrome oxidase subunit II (COII) specific RNA editing accessory factor. Sprehe M, Fisk JC, McEvoy SM, Read LK, Schumacher MA. UT MD Anderson Cancer Center, United States; Abstract k-RNA editing is a complex process in the mitochondria of kinetoplastid protozoa, including Trypanosoma brucei, that involves the guide-RNA directed insertion and deletion of uridines from precursor-mRNAs to produce mature, translatable mRNAs. k-RNA editing is performed by multiprotein complexes called editosomes. Additional non-editosome components termed k-RNA editing accessory factors affect the extent of editing of specific RNAs or classes of RNAs. The T. brucei p22 protein was identified as one such accessory factor. Here we show that p22 contributes to cell growth in the procyclic form of T. brucei and functions as a COII-specific k-RNA editing accessory factor. To gain insight into its functions, we solved the crystal structure of the T. brucei p22 protein to 2.0 Angstrom resolution. The p22 structure consists of a six stranded, antiparallel beta-sheet flanked by five alpha-helices. Three p22 subunits combine to form a tight trimer that is primarily stabilized by interactions between helical residues. One side of the trimer is strikingly acidic while the opposite face is more neutral. Database searches show p22 is structurally similar to human p32, which has a number of functions including regulation of RNA splicing. p32 interacts with a number of target proteins via its alpha1 N-terminal helix, which is among the most conserved regions between p22 and p32. Co-IP studies showed that p22 interacts with the editosome and the k-RNA accessory protein, TbRGG2 and alpha1 of p22 was shown to be important for the p22-TbRGG2 interaction. Thus, these combined studies suggest that p22 mediates its role in k-RNA editing by acting as an adaptor protein.
	PMID: 20392699 [PubMed - as supplied by publisher]
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