Isolation and characterization of Plasmodium falciparum UAP56 homolog: evidence for the coupling of RNA binding and splicing activity by site-directed mutations

Archives of Biochemistry and Biophysics
Jay ShankarRenu Tuteja

Abstract

UAP56 (U2AF65 associated protein) is a member of the DEAD-box helicase family. Helicases are essential enzymes generally involved in the metabolism of nucleic acids. The gene encoding a member of DEAD-box family was cloned and characterized from the human malaria parasite Plasmodium falciparum. PfU52 is homologous to UAP56 and contains the RNA-dependent ATPase, RNA helicase and RNA binding activities. Using the parasite extract we report that PfU52 is involved in splicing reaction. Site-directed mutagenesis studies indicate that the conserved residues glycine 181, isoleucine 182 and arginine 206 are involved in RNA binding and this activity is required for the enzymatic activities of PfU52. PfU52 is expressed in all the intraerythrocytic developmental stages of the parasite. In the present study we have reported the detailed characterization of PfU52 from P. falciparum and these results advance the knowledge regarding the function of UAP56 in general.

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Citations

Jun 9, 2014·Plant Molecular Biology·Narendra TutejaRenu Tuteja
Oct 15, 2011·Parasitology International·Renu Tuteja
Nov 5, 2011·Journal of Molecular Biology·Stephen P EdgcombJames R Williamson
Dec 3, 2014·Molecular and Biochemical Parasitology·Chayaphat WongsombatPhilip J Shaw
Aug 21, 2016·Molecular Microbiology·Mariana SerpeloniAndréa R Ávila
May 14, 2017·The FEBS Journal·Renu Tuteja
Nov 6, 2015·The Korean Journal of Parasitology·Laurence A MarchatCesar Lopez-Camarillo
Nov 4, 2015·BMC Genomics·B P Niranjan ReddyScott E Lindner
Aug 28, 2010·Communicative & Integrative Biology·Renu Tuteja, Jatin Mehta
Dec 21, 2010·Molecular and Biochemical Parasitology·Jatin Mehta, Renu Tuteja

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